ID   GANP_HUMAN              Reviewed;        1980 AA.
AC   O60318; C9JL56; Q2M3C1; Q6PJP6; Q9BSY5; Q9UMT4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   09-DEC-2015, entry version 135.
DE   RecName: Full=Germinal-center associated nuclear protein;
DE            Short=GANP;
DE   AltName: Full=80 kDa MCM3-associated protein;
DE   AltName: Full=MCM3 acetylating protein;
DE            Short=MCM3AP;
DE            EC=2.3.1.-;
DE   AltName: Full=MCM3 acetyltransferase;
GN   Name=MCM3AP; Synonyms=GANP, KIAA0572, MAP80;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11024281; DOI=10.1016/S0378-1119(00)00336-X;
RA   Abe E., Kuwahara K., Yoshida M., Suzuki M., Terasaki H., Matsuo Y.,
RA   Takahashi E., Sakaguchi N.;
RT   "Structure, expression, and chromosomal localization of the human gene
RT   encoding a germinal center-associated nuclear protein (GANP) that
RT   associates with MCM3 involved in the initiation of DNA replication.";
RL   Gene 255:219-227(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-102; VAL-288;
RP   LEU-333; LEU-413; LEU-1051; MET-1062; TRP-1314; GLU-1449; ILE-1576;
RP   THR-1795; ARG-1870 AND VAL-1941.
RG   NIEHS SNPs program;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA   Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA   Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA   Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA   Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA   Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA   Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA   Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA   Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA   Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA   Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA   Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-102.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-1980.
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX.
RT   The complete sequences of 100 new cDNA clones from brain which can
RT   code for large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1260-1980.
RX   PubMed=9712829; DOI=10.1074/jbc.273.35.22177;
RA   Takei Y., Tsujimoto G.;
RT   "Identification of a novel MCM3-associated protein that facilitates
RT   MCM3 nuclear localization.";
RL   J. Biol. Chem. 273:22177-22180(1998).
RN   [7]
RP   FUNCTION (ISOFORM MCM3AP), SUBCELLULAR LOCATION (ISOFORM MCM3AP),
RP   INTERACTION WITH MCM3, AND MUTAGENESIS OF 1730-HIS--GLY-1733.
RX   PubMed=11258703; DOI=10.1093/embo-reports/kve026;
RA   Takei Y., Swietlik M., Tanoue A., Tsujimoto G., Kouzarides T.,
RA   Laskey R.;
RT   "MCM3AP, a novel acetyltransferase that acetylates replication protein
RT   MCM3.";
RL   EMBO Rep. 2:119-123(2001).
RN   [8]
RP   FUNCTION (ISOFORM MCM3AP).
RX   PubMed=12226073; DOI=10.1074/jbc.C200442200;
RA   Takei Y., Assenberg M., Tsujimoto G., Laskey R.;
RT   "The MCM3 acetylase MCM3AP inhibits initiation, but not elongation, of
RT   DNA replication via interaction with MCM3.";
RL   J. Biol. Chem. 277:43121-43125(2002).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   FUNCTION (ISOFORM GANP), SUBCELLULAR LOCATION, FG-REPEATS, AND
RP   INTERACTION WITH NXF1.
RX   PubMed=20005110; DOI=10.1016/j.cub.2009.10.078;
RA   Wickramasinghe V.O., McMurtrie P.I., Mills A.D., Takei Y.,
RA   Penrhyn-Lowe S., Amagase Y., Main S., Marr J., Stewart M.,
RA   Laskey R.A.;
RT   "mRNA export from mammalian cell nuclei is dependent on GANP.";
RL   Curr. Biol. 20:25-31(2010).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [14]
RP   ALTERNATIVE PROMOTER USAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=21195085; DOI=10.1016/j.jmb.2010.12.035;
RA   Wickramasinghe V.O., McMurtrie P.I., Marr J., Amagase Y., Main S.,
RA   Mills A.D., Laskey R.A., Takei Y.;
RT   "MCM3AP is transcribed from a promoter within an intron of the
RT   overlapping gene for GANP.";
RL   J. Mol. Biol. 406:355-361(2011).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1163-1235 IN COMPLEX WITH
RP   ENY2, FUNCTION, SUBUNIT, IDENTIFICATION IN THE TREX-2 COMPLEX, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=22307388; DOI=10.1093/nar/gks059;
RA   Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M.,
RA   Wickramasinghe V.O.;
RT   "Functional and structural characterization of the mammalian TREX-2
RT   complex that links transcription with nuclear messenger RNA export.";
RL   Nucleic Acids Res. 40:4562-4573(2012).
RN   [17]
RP   VARIANTS [LARGE SCALE ANALYSIS] VAL-409 AND ILE-1576.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [18]
RP   VARIANT LYS-915.
RX   PubMed=24123876; DOI=10.1136/jmedgenet-2013-101644;
RA   Schuurs-Hoeijmakers J.H., Vulto-van Silfhout A.T., Vissers L.E.,
RA   van de Vondervoort I.I., van Bon B.W., de Ligt J., Gilissen C.,
RA   Hehir-Kwa J.Y., Neveling K., del Rosario M., Hira G., Reitano S.,
RA   Vitello A., Failla P., Greco D., Fichera M., Galesi O., Kleefstra T.,
RA   Greally M.T., Ockeloen C.W., Willemsen M.H., Bongers E.M.,
RA   Janssen I.M., Pfundt R., Veltman J.A., Romano C., Willemsen M.A.,
RA   van Bokhoven H., Brunner H.G., de Vries B.B., de Brouwer A.P.;
RT   "Identification of pathogenic gene variants in small families with
RT   intellectually disabled siblings by exome sequencing.";
RL   J. Med. Genet. 50:802-811(2013).
CC   -!- FUNCTION: Isoform GANP: Essential for the generation of high-
CC       affinity B-cells against T-cell-dependent antigens by affecting
CC       somatic hypermutation at the IgV-regions. May have stimulation-
CC       dependent DNA primase activity that would generate extra RNA
CC       primers in very rapidely proliferating cells and would support
CC       clonal expansion of differentiating B-cells (By similarity).
CC       Involved in the nuclear export of poly(A)-containing mRNAs by
CC       acting as a scaffold for the TREX-2 complex. The TREX-2 complex
CC       functions in docking export-competent ribonucleoprotein particles
CC       (mRNPs) to the nuclear entrance of the nuclear pore complex
CC       (nuclear basket). TREX-2 participates in mRNA export and accurate
CC       chromatin positioning in the nucleus by tethering genes to the
CC       nuclear periphery. {ECO:0000250, ECO:0000269|PubMed:22307388}.
CC   -!- FUNCTION: Isoform MCM3AP: Acetyltransferase targeting MCM3.
CC       Inhibits initiation of DNA replication, but not elongation.
CC       {ECO:0000269|PubMed:22307388}.
CC   -!- SUBUNIT: Interacts with AICDA/AID (By similarity). Component of
CC       the nuclear pore complex (NPC)-associated TREX-2 complex
CC       (transcription and export complex 2), composed of at least GANP,
CC       two copies of ENY2, PCID2, DSS1, and either centrin CETN2 or
CC       CETN3. Isoform MCM3AP interacts with MCM3. Interacts with NXF1 (By
CC       via FG-repeats). {ECO:0000250, ECO:0000269|PubMed:11258703,
CC       ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:22307388}.
CC   -!- SUBCELLULAR LOCATION: Isoform GANP: Cytoplasm. Nucleus envelope.
CC       Nucleus, nuclear pore complex. Note=In B-cells nuclear import
CC       depends on interaction with AICDA/AID, and GANP is selectively
CC       targeted to the IgV-region gene. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Isoform MCM3AP: Cytoplasm
CC       {ECO:0000269|PubMed:11258703}. Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:11258703}. Note=Binding to MCM3 is required
CC       for nuclear import, associates with chromatin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=GANP;
CC         IsoId=O60318-1; Sequence=Displayed;
CC       Name=MCM3AP; Synonyms=80 kDa MCM3-associated protein;
CC         IsoId=O60318-2; Sequence=VSP_053438;
CC         Note=Produced via an alternative promoter within an intron of
CC         GANP. MCM3AP promoter elements are poorly conserved in mice,
CC         suggesting that the regulation of MCM3AP may be human specific.;
CC   -!- PTM: Phosphorylation at Ser-508 by CDKs is required for DNA
CC       primase activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SAC3 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/mcm3ap/";
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DR   EMBL; AJ010089; CAB52687.1; -; mRNA.
DR   EMBL; AY590469; AAS89300.1; -; Genomic_DNA.
DR   EMBL; AP000471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013285; AAH13285.2; -; mRNA.
DR   EMBL; BC004497; AAH04497.2; -; mRNA.
DR   EMBL; BC104958; AAI04959.1; -; mRNA.
DR   EMBL; BC104960; AAI04961.1; -; mRNA.
DR   EMBL; AB011144; BAA25498.1; -; mRNA.
DR   EMBL; AB005543; BAA25170.1; -; mRNA.
DR   CCDS; CCDS13734.1; -. [O60318-1]
DR   PIR; T00339; T00339.
DR   RefSeq; NP_003897.2; NM_003906.4. [O60318-1]
DR   RefSeq; XP_005261260.1; XM_005261203.3. [O60318-1]
DR   RefSeq; XP_005261261.1; XM_005261204.3. [O60318-1]
DR   RefSeq; XP_005261262.1; XM_005261205.2. [O60318-1]
DR   RefSeq; XP_005261263.1; XM_005261206.3. [O60318-1]
DR   RefSeq; XP_006724127.1; XM_006724064.2. [O60318-1]
DR   UniGene; Hs.389037; -.
DR   UniGene; Hs.592438; -.
DR   PDB; 4DHX; X-ray; 2.10 A; A/D=1163-1235.
DR   PDBsum; 4DHX; -.
DR   ProteinModelPortal; O60318; -.
DR   SMR; O60318; 1163-1234.
DR   BioGrid; 114406; 26.
DR   DIP; DIP-31696N; -.
DR   IntAct; O60318; 33.
DR   MINT; MINT-1180375; -.
DR   STRING; 9606.ENSP00000291688; -.
DR   TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR   PhosphoSite; O60318; -.
DR   BioMuta; MCM3AP; -.
DR   MaxQB; O60318; -.
DR   PaxDb; O60318; -.
DR   PeptideAtlas; O60318; -.
DR   PRIDE; O60318; -.
DR   Ensembl; ENST00000291688; ENSP00000291688; ENSG00000160294. [O60318-1]
DR   Ensembl; ENST00000397708; ENSP00000380820; ENSG00000160294. [O60318-1]
DR   GeneID; 8888; -.
DR   KEGG; hsa:8888; -.
DR   UCSC; uc002zir.1; human. [O60318-1]
DR   CTD; 8888; -.
DR   GeneCards; MCM3AP; -.
DR   H-InvDB; HIX0016189; -.
DR   HGNC; HGNC:6946; MCM3AP.
DR   HPA; HPA021527; -.
DR   HPA; HPA032103; -.
DR   MIM; 603294; gene.
DR   neXtProt; NX_O60318; -.
DR   PharmGKB; PA30692; -.
DR   eggNOG; KOG1860; Eukaryota.
DR   eggNOG; COG5079; LUCA.
DR   GeneTree; ENSGT00530000063781; -.
DR   HOGENOM; HOG000113500; -.
DR   HOVERGEN; HBG052431; -.
DR   InParanoid; O60318; -.
DR   OMA; FCASEAE; -.
DR   OrthoDB; EOG78D7JB; -.
DR   PhylomeDB; O60318; -.
DR   TreeFam; TF105948; -.
DR   ChiTaRS; MCM3AP; human.
DR   GeneWiki; MCM3AP; -.
DR   GenomeRNAi; 8888; -.
DR   NextBio; 33379; -.
DR   PRO; PR:O60318; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   Bgee; O60318; -.
DR   CleanEx; HS_MCM3AP; -.
DR   ExpressionAtlas; O60318; baseline and differential.
DR   Genevisible; O60318; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006606; P:protein import into nucleus; TAS:ProtInc.
DR   InterPro; IPR031910; GANP_CID_dom.
DR   InterPro; IPR031907; MCM3AP_GANP.
DR   InterPro; IPR031908; NupH_GANP.
DR   InterPro; IPR005062; SAC3/GANP/THP3.
DR   Pfam; PF16766; CID_GANP; 1.
DR   Pfam; PF16769; MCM3AP_GANP; 1.
DR   Pfam; PF16768; NupH_GANP; 1.
DR   Pfam; PF03399; SAC3_GANP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase;
KW   Alternative promoter usage; Coiled coil; Complete proteome; Cytoplasm;
KW   Immunity; mRNA transport; Nuclear pore complex; Nucleus;
KW   Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW   Transferase; Translocation; Transport.
FT   CHAIN         1   1980       Germinal-center associated nuclear
FT                                protein.
FT                                /FTId=PRO_0000096284.
FT   REGION       33    340       FG-repeats.
FT   REGION      421    557       DNA primase.
FT   REGION      636    990       SAC3 homology.
FT   REGION     1162   1256       CID.
FT   REGION     1658   1790       Acetyltransferase.
FT   COILED     1133   1170       {ECO:0000255}.
FT   MOD_RES     489    489       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9WUU9}.
FT   MOD_RES     490    490       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9WUU9}.
FT   MOD_RES     508    508       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9WUU9}.
FT   MOD_RES     538    538       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   VAR_SEQ       1   1259       Missing (in isoform MCM3AP).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_053438.
FT   VARIANT     102    102       S -> L (in dbSNP:rs9975588).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019240.
FT   VARIANT     288    288       M -> V (in dbSNP:rs17182545).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019241.
FT   VARIANT     333    333       R -> L (in dbSNP:rs17182552).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019242.
FT   VARIANT     409    409       L -> V (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035472.
FT   VARIANT     413    413       P -> L (in dbSNP:rs17182566).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019243.
FT   VARIANT     915    915       E -> K (found in a patient with border-
FT                                line to mild intellectual disability,
FT                                progressive polyneuropathy and ptosis;
FT                                unknown pathological significance).
FT                                {ECO:0000269|PubMed:24123876}.
FT                                /FTId=VAR_070560.
FT   VARIANT    1051   1051       P -> L (in dbSNP:rs17182850).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019244.
FT   VARIANT    1062   1062       V -> M (in dbSNP:rs17182857).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019245.
FT   VARIANT    1314   1314       R -> W (in dbSNP:rs17176709).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019246.
FT   VARIANT    1449   1449       D -> E (in dbSNP:rs17183220).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019247.
FT   VARIANT    1576   1576       V -> I (in dbSNP:rs17183248).
FT                                {ECO:0000269|PubMed:16959974,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019248.
FT   VARIANT    1795   1795       A -> T (in dbSNP:rs17183290).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019249.
FT   VARIANT    1831   1831       R -> C (in dbSNP:rs2298697).
FT                                /FTId=VAR_053973.
FT   VARIANT    1870   1870       L -> R (in dbSNP:rs17176933).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019250.
FT   VARIANT    1941   1941       A -> V (in dbSNP:rs17183403).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019251.
FT   MUTAGEN    1730   1733       HGAG->AAAA: Severely decreased MCM3
FT                                acetylating activity.
FT                                {ECO:0000269|PubMed:11258703}.
FT   HELIX      1168   1232       {ECO:0000244|PDB:4DHX}.
SQ   SEQUENCE   1980 AA;  218405 MW;  503D192686FC38A8 CRC64;
     MNPTNPFSGQ QPSAFSASSS NVGTLPSKPP FRFGQPSLFG QNSTLSGKSS GFSQVSSFPA
     SSGVSHSSSV QTLGFTQTSS VGPFSGLEHT STFVATSGPS SSSVLGNTGF SFKSPTSVGA
     FPSTSAFGQE AGEIVNSGFG KTEFSFKPLE NAVFKPILGA ESEPEKTQSQ IASGFFTFSH
     PISSAPGGLA PFSFPQVTSS SATTSNFTFS KPVSSNNSLS AFTPALSNQN VEEEKRGPKS
     IFGSSNNSFS SFPVSSAVLG EPFQASKAGV RQGCEEAVSQ VEPLPSLMKG LKRKEDQDRS
     PRRHGHEPAE DSDPLSRGDH PPDKRPVRLN RPRGGTLFGR TIQDVFKSNK EVGRLGNKEA
     KKETGFVESA ESDHMAIPGG NQSVLAPSRI PGVNKEEETE SREKKEDSLR GTPARQSNRS
     ESTDSLGGLS PSEVTAIQCK NIPDYLNDRT ILENHFGKIA KVQRIFTRRS KKLAVVHFFD
     HASAALARKK GKSLHKDMAI FWHRKKISPN KKPFSLKEKK PGDGEVSPST EDAPFQHSPL
     GKAAGRTGAS SLLNKSSPVK KPSLLKAHQF EGDSFDSASE GSEGLGPCVL SLSTLIGTVA
     ETSKEKYRLL DQRDRIMRQA RVKRTDLDKA RTFVGTCLDM CPEKERYMRE TRSQLSVFEV
     VPGTDQVDHA AAVKEYSRSS ADQEEPLPHE LRPLPVLSRT MDYLVTQIMD QKEGSLRDWY
     DFVWNRTRGI RKDITQQHLC DPLTVSLIEK CTRFHIHCAH FMCEEPMSSF DAKINNENMT
     KCLQSLKEMY QDLRNKGVFC ASEAEFQGYN VLLSLNKGDI LREVQQFHPA VRNSSEVKFA
     VQAFAALNSN NFVRFFKLVQ SASYLNACLL HCYFSQIRKD ALRALNFAYT VSTQRSTIFP
     LDGVVRMLLF RDCEEATDFL TCHGLTVSDG CVELNRSAFL EPEGLSKTRK SVFITRKLTV
     SVGEIVNGGP LPPVPRHTPV CSFNSQNKYI GESLAAELPV STQRPGSDTV GGGRGEECGV
     EPDAPLSSLP QSLPAPAPSP VPLPPVLALT PSVAPSLFQL SVQPEPPPPE PVPMYSDEDL
     AQVVDELIQE ALQRDCEEVG SAGAAYAAAA LGVSNAAMED LLTAATTGIL RHIAAEEVSK
     ERERREQERQ RAEEERLKQE RELVLSELSQ GLAVELMERV MMEFVRETCS QELKNAVETD
     QRVRVARCCE DVCAHLVDLF LVEEIFQTAK ETLQELQCFC KYLQRWREAV TARKKLRRQM
     RAFPAAPCCV DVSDRLRALA PSAECPIAEE NLARGLLDLG HAGRLGISCT RLRRLRNKTA
     HQMKVQHFYQ QLLSDVAWAS LDLPSLVAEH LPGRQEHVFW KLVLVLPDVE EQSPESCGRI
     LANWLKVKFM GDEGSVDDTS SDAGGIQTLS LFNSLSSKGD QMISVNVCIK VAHGALSDGA
     IDAVETQKDL LGASGLMLLL PPKMKSEDMA EEDVYWLSAL LQLKQLLQAK PFQPALPLVV
     LVPSPGGDAV EKEVEDGLML QDLVSAKLIS DYTVTEIPDT INDLQGSTKV LQAVQWLVSH
     CPHSLDLCCQ TLIQYVEDGI GHEFSGRFFH DRRERRLGGL ASQEPGAIIE LFNSVLQFLA
     SVVSSEQLCD LSWPVTEFAE AGGSRLLPHL HWNAPEHLAW LKQAVLGFQL PQMDLPPLGA
     PWLPVCSMVV QYASQIPSSR QTQPVLQSQV ENLLHRTYCR WKSKSPSPVH GAGPSVMEIP
     WDDLIALCIN HKLRDWTPPR LPVTSEALSE DGQICVYFFK NDLKKYDVPL SWEQARLQTQ
     KELQLREGRL AIKPFHPSAN NFPIPLLHMH RNWKRSTECA QEGRIPSTED LMRGASAEEL
     LAQCLSSSLL LEKEENKRFE DQLQQWLSED SGAFTDLTSL PLYLPQTLVS LSHTIEPVMK
     TSVTTSPQSD MMREQLQLSE ATGTCLGERL KHLERLIRSS REEEVASELH LSALLDMVDI
//