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P33991

- MCM4_HUMAN

UniProt

P33991 - MCM4_HUMAN

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Protein

DNA replication licensing factor MCM4

Gene

MCM4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi510 – 5178ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA helicase activity Source: Ensembl
  3. single-stranded DNA binding Source: Ensembl

GO - Biological processi

  1. DNA replication Source: UniProtKB
  2. DNA replication initiation Source: InterPro
  3. DNA strand elongation involved in DNA replication Source: Reactome
  4. DNA unwinding involved in DNA replication Source: Ensembl
  5. G1/S transition of mitotic cell cycle Source: Reactome
  6. mitotic cell cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1156. Orc1 removal from chromatin.
REACT_207. Removal of licensing factors from origins.
REACT_2148. Switching of origins to a post-replicative state.
REACT_2243. Assembly of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.
REACT_6776. Unwinding of DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM4 (EC:3.6.4.12)
Alternative name(s):
CDC21 homolog
P1-CDC21
Gene namesi
Name:MCM4
Synonyms:CDC21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:6947. MCM4.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. MCM complex Source: UniProtKB
  2. membrane Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Natural killer cell and glucocorticoid deficiency with DNA repair defect (NKGCD) [MIM:609981]: An autosomal recessive disorder characterized by severe intra- and extrauterine growth retardation, microcephaly, decreased numbers of natural killer cells, and recurrent viral infections, most often affecting the respiratory tract and leading to respiratory failure. Affected individuals also have adrenal insufficiency requiring corticosteroid replacement therapy and may have an increased susceptibility to cancer.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi609981. phenotype.
Orphaneti75391. Immunodeficiency with natural-killer cell deficiency and adrenal insufficiency.
PharmGKBiPA30694.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 863862DNA replication licensing factor MCM4PRO_0000194101Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei26 – 261Phosphoserine1 Publication
Modified residuei31 – 311Phosphoserine1 Publication
Modified residuei32 – 321Phosphoserine2 Publications
Modified residuei34 – 341Phosphoserine1 Publication
Modified residuei120 – 1201Phosphoserine4 Publications
Modified residuei131 – 1311Phosphoserine3 Publications
Modified residuei142 – 1421Phosphoserine1 Publication
Modified residuei145 – 1451Phosphoserine1 Publication
Modified residuei220 – 2201N6-acetyllysine1 Publication
Modified residuei450 – 4501N6-acetyllysine1 Publication
Modified residuei858 – 8581N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP33991.
PaxDbiP33991.
PeptideAtlasiP33991.
PRIDEiP33991.

PTM databases

PhosphoSiteiP33991.

Miscellaneous databases

PMAP-CutDBP33991.

Expressioni

Gene expression databases

BgeeiP33991.
CleanExiHS_MCM4.
ExpressionAtlasiP33991. baseline and differential.
GenevestigatoriP33991.

Organism-specific databases

HPAiCAB004497.
HPA004873.
HPA031052.

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 (By simililarity). Interacts with MCMBP.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MCM7P3399314EBI-374938,EBI-355924
MCMBPQ9BTE314EBI-374938,EBI-749378
ORFQ9Q2G43EBI-374938,EBI-6248094From a different organism.
SSRP1Q089455EBI-374938,EBI-353771
SUPT16HQ9Y5B93EBI-374938,EBI-1046849

Protein-protein interaction databases

BioGridi110341. 67 interactions.
DIPiDIP-31729N.
IntActiP33991. 49 interactions.
MINTiMINT-1202120.
STRINGi9606.ENSP00000262105.

Structurei

3D structure databases

ProteinModelPortaliP33991.
SMRiP33991. Positions 167-766.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini458 – 667210MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi642 – 6454Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1241.
GeneTreeiENSGT00770000120580.
HOGENOMiHOG000224127.
HOVERGENiHBG102781.
InParanoidiP33991.
KOiK02212.
OMAiMHSSAIP.
OrthoDBiEOG78D7JF.
PhylomeDBiP33991.
TreeFamiTF300463.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR008047. MCM_4.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01660. MCMPROTEIN4.
SMARTiSM00382. AAA. 1 hit.
SM00350. 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.

P33991-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSPASTPSR RGSRRGRATP AQTPRSEDAR SSPSQRRRGE DSTSTGELQP
60 70 80 90 100
MPTSPGVDLQ SPAAQDVLFS SPPQMHSSAI PLDFDVSSPL TYGTPSSRVE
110 120 130 140 150
GTPRSGVRGT PVRQRPDLGS AQKGLQVDLQ SDGAAAEDIV ASEQSLGQKL
160 170 180 190 200
VIWGTDVNVA ACKENFQRFL QRFIDPLAKE EENVGIDITE PLYMQRLGEI
210 220 230 240 250
NVIGEPFLNV NCEHIKSFDK NLYRQLISYP QEVIPTFDMA VNEIFFDRYP
260 270 280 290 300
DSILEHQIQV RPFNALKTKN MRNLNPEDID QLITISGMVI RTSQLIPEMQ
310 320 330 340 350
EAFFQCQVCA HTTRVEMDRG RIAEPSVCGR CHTTHSMALI HNRSLFSDKQ
360 370 380 390 400
MIKLQESPED MPAGQTPHTV ILFAHNDLVD KVQPGDRVNV TGIYRAVPIR
410 420 430 440 450
VNPRVSNVKS VYKTHIDVIH YRKTDAKRLH GLDEEAEQKL FSEKRVELLK
460 470 480 490 500
ELSRKPDIYE RLASALAPSI YEHEDIKKGI LLQLFGGTRK DFSHTGRGKF
510 520 530 540 550
RAEINILLCG DPGTSKSQLL QYVYNLVPRG QYTSGKGSSA VGLTAYVMKD
560 570 580 590 600
PETRQLVLQT GALVLSDNGI CCIDEFDKMN ESTRSVLHEV MEQQTLSIAK
610 620 630 640 650
AGIICQLNAR TSVLAAANPI ESQWNPKKTT IENIQLPHTL LSRFDLIFLL
660 670 680 690 700
LDPQDEAYDR RLAHHLVALY YQSEEQAEEE LLDMAVLKDY IAYAHSTIMP
710 720 730 740 750
RLSEEASQAL IEAYVDMRKI GSSRGMVSAY PRQLESLIRL AEAHAKVRLS
760 770 780 790 800
NKVEAIDVEE AKRLHREALK QSATDPRTGI VDISILTTGM SATSRKRKEE
810 820 830 840 850
LAEALKKLIL SKGKTPALKY QQLFEDIRGQ SDIAITKDMF EEALRALADD
860
DFLTVTGKTV RLL
Length:863
Mass (Da):96,558
Last modified:May 10, 2005 - v5
Checksum:i96D9CA2A7D88D015
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621P → T in CAA52801. (PubMed:7601140)Curated
Sequence conflicti206 – 2061P → Q in CAA52801. (PubMed:7601140)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti460 – 4601E → G.1 Publication
Corresponds to variant rs17287663 [ dbSNP | Ensembl ].
VAR_020500
Natural varianti650 – 6501L → M.3 Publications
Corresponds to variant rs762679 [ dbSNP | Ensembl ].
VAR_020501

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74794 mRNA. Translation: CAA52801.1.
AY588245 Genomic DNA. Translation: AAS83108.1.
BC031061 mRNA. Translation: AAH31061.1.
U63630 Genomic DNA. Translation: AAC52018.1.
U90415 Genomic DNA. Translation: AAB51723.3.
CCDSiCCDS6143.1.
PIRiS65954.
RefSeqiNP_005905.2. NM_005914.3.
NP_877423.1. NM_182746.2.
UniGeneiHs.460184.

Genome annotation databases

EnsembliENST00000262105; ENSP00000262105; ENSG00000104738.
ENST00000523944; ENSP00000430194; ENSG00000104738.
GeneIDi4173.
KEGGihsa:4173.
UCSCiuc003xqk.2. human.

Polymorphism databases

DMDMi68571766.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74794 mRNA. Translation: CAA52801.1 .
AY588245 Genomic DNA. Translation: AAS83108.1 .
BC031061 mRNA. Translation: AAH31061.1 .
U63630 Genomic DNA. Translation: AAC52018.1 .
U90415 Genomic DNA. Translation: AAB51723.3 .
CCDSi CCDS6143.1.
PIRi S65954.
RefSeqi NP_005905.2. NM_005914.3.
NP_877423.1. NM_182746.2.
UniGenei Hs.460184.

3D structure databases

ProteinModelPortali P33991.
SMRi P33991. Positions 167-766.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110341. 67 interactions.
DIPi DIP-31729N.
IntActi P33991. 49 interactions.
MINTi MINT-1202120.
STRINGi 9606.ENSP00000262105.

PTM databases

PhosphoSitei P33991.

Polymorphism databases

DMDMi 68571766.

Proteomic databases

MaxQBi P33991.
PaxDbi P33991.
PeptideAtlasi P33991.
PRIDEi P33991.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262105 ; ENSP00000262105 ; ENSG00000104738 .
ENST00000523944 ; ENSP00000430194 ; ENSG00000104738 .
GeneIDi 4173.
KEGGi hsa:4173.
UCSCi uc003xqk.2. human.

Organism-specific databases

CTDi 4173.
GeneCardsi GC08P048873.
H-InvDB HIX0007492.
HGNCi HGNC:6947. MCM4.
HPAi CAB004497.
HPA004873.
HPA031052.
MIMi 602638. gene.
609981. phenotype.
neXtProti NX_P33991.
Orphaneti 75391. Immunodeficiency with natural-killer cell deficiency and adrenal insufficiency.
PharmGKBi PA30694.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1241.
GeneTreei ENSGT00770000120580.
HOGENOMi HOG000224127.
HOVERGENi HBG102781.
InParanoidi P33991.
KOi K02212.
OMAi MHSSAIP.
OrthoDBi EOG78D7JF.
PhylomeDBi P33991.
TreeFami TF300463.

Enzyme and pathway databases

Reactomei REACT_1095. Activation of the pre-replicative complex.
REACT_1156. Orc1 removal from chromatin.
REACT_207. Removal of licensing factors from origins.
REACT_2148. Switching of origins to a post-replicative state.
REACT_2243. Assembly of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.
REACT_6776. Unwinding of DNA.

Miscellaneous databases

ChiTaRSi MCM4. human.
GeneWikii MCM4.
GenomeRNAii 4173.
NextBioi 16436.
PMAP-CutDB P33991.
PROi P33991.
SOURCEi Search...

Gene expression databases

Bgeei P33991.
CleanExi HS_MCM4.
ExpressionAtlasi P33991. baseline and differential.
Genevestigatori P33991.

Family and domain databases

Gene3Di 2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR008047. MCM_4.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view ]
Pfami PF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view ]
PRINTSi PR01657. MCMFAMILY.
PR01660. MCMPROTEIN4.
SMARTi SM00382. AAA. 1 hit.
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

« Hide 'large scale' publications
  1. "A human homologue of the yeast replication protein Cdc21. Interactions with other Mcm proteins."
    Musahl C., Schulte D., Burkhart R., Knippers R.
    Eur. J. Biochem. 230:1096-1101(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-650.
  2. NIEHS SNPs program
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-460.
  3. "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], VARIANT MET-650.
    Tissue: Testis.
  4. "The promoters for human DNA-PKcs (PRKDC) and MCM4: divergently transcribed genes located at chromosome 8 band q11."
    Connelly M.A., Zhang H., Kieleczawa J., Anderson C.W.
    Genomics 47:71-83(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-712.
  5. "MCM4 and PRKDC, human genes encoding proteins MCM4 and DNA-PKcs, are close neighbours located on chromosome 8q12-->q13."
    Ladenburger E.M., Fackelmayer F.O., Hameister H., Knippers R.
    Cytogenet. Cell Genet. 77:268-270(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-23.
  6. "The P1 family: a new class of nuclear mammalian proteins related to the yeast Mcm replication proteins."
    Hu B., Burkhart R., Schulte D., Musahl C., Knippers R.
    Nucleic Acids Res. 21:5289-5293(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 440-863, VARIANT MET-650.
    Tissue: Cervix.
  7. "A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex."
    Ishimi Y.
    J. Biol. Chem. 272:24508-24513(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Essential role of phosphorylation of MCM2 by Cdc7/Dbf4 in the initiation of DNA replication in mammalian cells."
    Tsuji T., Ficarro S.B., Jiang W.
    Mol. Biol. Cell 17:4459-4472(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, ATPASE ACTIVITY OF THE MCM2-7 COMPLEX.
  10. "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] [Europe PMC] [Abstract]
    Cited for: HELICASE ACTIVITY OF THE MCM2-3 COMPLEX, INTERACTION WITH MCMBP, IDENTIFICATION IN THE MCM2-7 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-31; SER-32 AND SER-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220 AND LYS-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-120; SER-131; SER-142 AND SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "MCM4 mutation causes adrenal failure, short stature, and natural killer cell deficiency in humans."
    Hughes C.R., Guasti L., Meimaridou E., Chuang C.H., Schimenti J.C., King P.J., Costigan C., Clark A.J., Metherell L.A.
    J. Clin. Invest. 122:814-820(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN NKGCD.
  19. Cited for: INVOLVEMENT IN NKGCD.
  20. "Recessive mutations in MCM4/PRKDC cause a novel syndrome involving a primary immunodeficiency and a disorder of DNA repair."
    Casey J.P., Nobbs M., McGettigan P., Lynch S., Ennis S.
    J. Med. Genet. 49:242-245(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN NKGCD.
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCM4_HUMAN
AccessioniPrimary (citable) accession number: P33991
Secondary accession number(s): Q8NEH1, Q99658
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 10, 2005
Last modified: November 26, 2014
This is version 154 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. Specifically a MCM467 subcomplex is shown to have in vitro helicase activity which is inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed physiological active complex.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3