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DNA helicase MCM9 (hMCM9) (EC 3.6.4.12) (Mini-chromosome maintenance deficient domain-containing protein 1) (Minichromosome maintenance 9)

 MCM9_HUMAN              Reviewed;        1143 AA.
Q9NXL9; B4DR30; B9DI77; Q2KHJ0; Q8N5S5; Q9HCV5;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
16-MAY-2012, sequence version 4.
18-JUL-2018, entry version 128.
RecName: Full=DNA helicase MCM9;
Short=hMCM9;
EC=3.6.4.12;
AltName: Full=Mini-chromosome maintenance deficient domain-containing protein 1;
AltName: Full=Minichromosome maintenance 9;
Name=MCM9; Synonyms=C6orf61, MCMDC1;
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 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 865-1143 (ISOFORM L).
TISSUE=Teratocarcinoma;
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 GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM S).
TISSUE=Brain;
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).
[4]
IDENTIFICATION.
PubMed=16226853; DOI=10.1016/j.gene.2005.07.031;
Lutzmann M., Maiorano D., Mechali M.;
"Identification of full genes and proteins of MCM9, a novel,
vertebrate-specific member of the MCM2-8 protein family.";
Gene 362:51-56(2005).
[5]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, 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).
[7]
FUNCTION, AND IDENTIFICATION IN THE MCM8-MCM9 COMPLEX.
PubMed=22771115; DOI=10.1016/j.molcel.2012.05.047;
Nishimura K., Ishiai M., Horikawa K., Fukagawa T., Takata M.,
Takisawa H., Kanemaki M.T.;
"Mcm8 and Mcm9 form a complex that functions in homologous
recombination repair induced by DNA interstrand crosslinks.";
Mol. Cell 47:511-522(2012).
[8]
ALTERNATIVE SPLICING (ISOFORM M), AND DEVELOPMENTAL STAGE.
PubMed=23403237; DOI=10.1016/j.gene.2013.01.054;
Jeffries E.P., Denq W.I., Bartko J.C., Trakselis M.A.;
"Identification, quantification, and evolutionary analysis of a novel
isoform of MCM9.";
Gene 519:41-49(2013).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762; SER-802 AND
SER-1109, 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).
[10]
INVOLVEMENT IN ODG4.
PubMed=25480036; DOI=10.1016/j.ajhg.2014.11.002;
Wood-Trageser M.A., Gurbuz F., Yatsenko S.A., Jeffries E.P.,
Kotan L.D., Surti U., Ketterer D.M., Matic J., Chipkin J., Jiang H.,
Trakselis M.A., Topaloglu A.K., Rajkovic A.;
"MCM9 mutations are associated with ovarian failure, short stature,
and chromosomal instability.";
Am. J. Hum. Genet. 95:754-762(2014).
-!- FUNCTION: Component of the MCM8-MCM9 complex, a complex involved
in homologous recombination repair following DNA interstrand
cross-links and plays a key role during gametogenesis. The MCM8-
MCM9 complex probably acts as a hexameric helicase downstream of
the Fanconi anemia proteins BRCA2 and RAD51 and is required to
process aberrant forks into homologous recombination substrates
and to orchestrate homologous recombination with resection, fork
stabilization and fork restart. {ECO:0000269|PubMed:22771115}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Component of the MCM8-MCM9 complex, which forms a hexamer
composed of MCM8 and MCM9. {ECO:0000269|PubMed:22771115}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to
nuclear foci and colocalizes with RAD51. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=L;
IsoId=Q9NXL9-1; Sequence=Displayed;
Note=Most abundant isoform.;
Name=M;
IsoId=Q9NXL9-2; Sequence=VSP_047462, VSP_047463;
Name=S;
IsoId=Q9NXL9-3; Sequence=VSP_028013, VSP_028014;
Name=4;
IsoId=Q9NXL9-4; Sequence=VSP_044180, VSP_044181;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: The expression of isoform L and isoform M is
cell cycle regulated: induced in S-phase, decreases through G2/M,
and becomes constant through G1. {ECO:0000269|PubMed:23403237}.
-!- DISEASE: Ovarian dysgenesis 4 (ODG4) [MIM:616185]: A disorder
characterized by lack of spontaneous pubertal development, primary
amenorrhea, uterine hypoplasia, and hypergonadotropic hypogonadism
as a result of streak gonads. {ECO:0000269|PubMed:25480036}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA90991.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG61142.1; Type=Erroneous termination; Positions=1070; Note=Translated as Lys.; Evidence={ECO:0000305};
Sequence=CAX30832.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK299076; BAG61142.1; ALT_SEQ; mRNA.
EMBL; AK000177; BAA90991.1; ALT_INIT; mRNA.
EMBL; AL132874; CAX30832.1; ALT_SEQ; Genomic_DNA.
EMBL; AL359634; CAX30832.1; JOINED; Genomic_DNA.
EMBL; BC031658; AAH31658.1; -; mRNA.
EMBL; BN000882; CAJ70648.1; -; mRNA.
CCDS; CCDS5121.1; -. [Q9NXL9-3]
CCDS; CCDS56447.1; -. [Q9NXL9-1]
RefSeq; NP_060166.2; NM_017696.2. [Q9NXL9-1]
RefSeq; NP_694987.1; NM_153255.4. [Q9NXL9-3]
UniGene; Hs.279008; -.
UniGene; Hs.733116; -.
UniGene; Hs.736853; -.
ProteinModelPortal; Q9NXL9; -.
SMR; Q9NXL9; -.
BioGrid; 129033; 37.
IntAct; Q9NXL9; 3.
STRING; 9606.ENSP00000314505; -.
iPTMnet; Q9NXL9; -.
PhosphoSitePlus; Q9NXL9; -.
BioMuta; MCM9; -.
DMDM; 387912921; -.
EPD; Q9NXL9; -.
MaxQB; Q9NXL9; -.
PaxDb; Q9NXL9; -.
PeptideAtlas; Q9NXL9; -.
PRIDE; Q9NXL9; -.
ProteomicsDB; 83112; -.
ProteomicsDB; 83113; -. [Q9NXL9-2]
DNASU; 254394; -.
Ensembl; ENST00000316068; ENSP00000312870; ENSG00000111877. [Q9NXL9-3]
Ensembl; ENST00000316316; ENSP00000314505; ENSG00000111877. [Q9NXL9-1]
Ensembl; ENST00000619706; ENSP00000480469; ENSG00000111877. [Q9NXL9-1]
GeneID; 254394; -.
KEGG; hsa:254394; -.
UCSC; uc003pyh.4; human. [Q9NXL9-1]
CTD; 254394; -.
DisGeNET; 254394; -.
EuPathDB; HostDB:ENSG00000111877.17; -.
GeneCards; MCM9; -.
HGNC; HGNC:21484; MCM9.
HPA; HPA031137; -.
MalaCards; MCM9; -.
MIM; 610098; gene.
MIM; 616185; phenotype.
neXtProt; NX_Q9NXL9; -.
OpenTargets; ENSG00000111877; -.
PharmGKB; PA162395071; -.
eggNOG; KOG0477; Eukaryota.
eggNOG; COG1241; LUCA.
GeneTree; ENSGT00920000149094; -.
HOGENOM; HOG000007282; -.
HOVERGEN; HBG108122; -.
InParanoid; Q9NXL9; -.
KO; K10738; -.
OMA; VMCAPEK; -.
OrthoDB; EOG091G01CK; -.
PhylomeDB; Q9NXL9; -.
TreeFam; TF329421; -.
ChiTaRS; MCM9; human.
GenomeRNAi; 254394; -.
PRO; PR:Q9NXL9; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000111877; -.
CleanEx; HS_MCM9; -.
ExpressionAtlas; Q9NXL9; baseline and differential.
Genevisible; Q9NXL9; HS.
GO; GO:0097362; C:MCM8-MCM9 complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0007292; P:female gamete generation; ISS:UniProtKB.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR031327; MCM.
InterPro; IPR001208; MCM_dom.
InterPro; IPR033762; MCM_OB.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11630; PTHR11630; 1.
Pfam; PF00493; MCM; 1.
Pfam; PF17207; MCM_OB; 1.
PRINTS; PR01657; MCMFAMILY.
SMART; SM00382; AAA; 1.
SMART; SM00350; MCM; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50051; MCM_2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; DNA damage;
DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 1143 DNA helicase MCM9.
/FTId=PRO_0000089513.
DOMAIN 300 505 MCM.
NP_BIND 352 359 ATP. {ECO:0000255}.
MOD_RES 762 762 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 802 802 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1109 1109 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 381 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044180.
VAR_SEQ 382 383 SA -> MS (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044181.
VAR_SEQ 383 391 AGLTVTAVK -> AGIVCDNFK (in isoform S).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028013.
VAR_SEQ 392 1143 Missing (in isoform S).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028014.
VAR_SEQ 606 648 GGALLGGVNALHTSFPENPGEQYQRQCELILEKLELQSLLS
EE -> VTESECAPIPTTGIGGRDYSRILEKWSRGRIKLQN
FITAGNQL (in isoform M). {ECO:0000305}.
/FTId=VSP_047462.
VAR_SEQ 649 1143 Missing (in isoform M). {ECO:0000305}.
/FTId=VSP_047463.
CONFLICT 433 433 Q -> R (in Ref. 1; BAG61142).
{ECO:0000305}.
CONFLICT 558 558 C -> S (in Ref. 1; BAG61142).
{ECO:0000305}.
CONFLICT 1063 1063 F -> V (in Ref. 1; BAA90991).
{ECO:0000305}.
CONFLICT 1136 1136 D -> G (in Ref. 1; BAA90991).
{ECO:0000305}.
SEQUENCE 1143 AA; 127313 MW; 3C35C8B3476A470F CRC64;
MNSDQVTLVG QVFESYVSEY HKNDILLILK ERDEDAHYPV VVNAMTLFET NMEIGEYFNM
FPSEVLTIFD SALRRSALTI LQSLSQPEAV SMKQNLHARI SGLPVCPELV REHIPKTKDV
GHFLSVTGTV IRTSLVKVLE FERDYMCNKC KHVFVIKADF EQYYTFCRPS SCPSLESCDS
SKFTCLSGLS SSPTRCRDYQ EIKIQEQVQR LSVGSIPRSM KVILEDDLVD SCKSGDDLTI
YGIVMQRWKP FQQDVRCEVE IVLKANYIQV NNEQSSGIIM DEEVQKEFED FWEYYKSDPF
AGRNVILASL CPQVFGMYLV KLAVAMVLAG GIQRTDATGT RVRGESHLLL VGDPGTGKSQ
FLKYAAKITP RSVLTTGIGS TSAGLTVTAV KDSGEWNLEA GALVLADAGL CCIDEFNSLK
EHDRTSIHEA MEQQTISVAK AGLVCKLNTR TTILAATNPK GQYDPQESVS VNIALGSPLL
SRFDLILVLL DTKNEDWDRI ISSFILENKG YPSKSEKLWS MEKMKTYFCL IRNLQPTLSD
VGNQVLLRYY QMQRQSDCRN AARTTIRLLE SLIRLAEAHA RLMFRDTVTL EDAITVVSVM
ESSMQGGALL GGVNALHTSF PENPGEQYQR QCELILEKLE LQSLLSEELR RLERLQNQSV
HQSQPRVLEV ETTPGSLRNG PGEESNFRTS SQQEINYSTH IFSPGGSPEG SPVLDPPPHL
EPNRSTSRKH SAQHKNNRDD SLDWFDFMAT HQSEPKNTVV VSPHPKTSGE NMASKISNST
SQGKEKSEPG QRSKVDIGLL PSPGETGVPW RADNVESNKK KRLALDSEAA VSADKPDSVL
THHVPRNLQK LCKERAQKLC RNSTRVPAQC TVPSHPQSTP VHSPDRMLDS PKRKRPKSLA
QVEEPAIENV KPPGSPVAKL AKFTFKQKSK LIHSFEDHSH VSPGATKIAV HSPKISQRRT
RRDAALPVKR PGKLTSTPGN QISSQPQGET KEVSQQPPEK HGPREKVMCA PEKRIIQPEL
ELGNETGCAH LTCEGDKKEE VSGSNKSGKV HACTLARLAN FCFTPPSESK SKSPPPERKN
RGERGPSSPP TTTAPMRVSK RKSFQLRGST EKLIVSKESL FTLPELGDEA FDCDWDEEMR
KKS


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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