Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P33992

- MCM5_HUMAN

UniProt

P33992 - MCM5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA replication licensing factor MCM5

Gene

MCM5

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 (By similarity). Interacts with MCMBP.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi381 – 3888ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. DNA helicase activity Source: InterPro

GO - Biological processi

  1. DNA replication Source: Reactome
  2. DNA replication initiation Source: InterPro
  3. DNA strand elongation involved in DNA replication Source: Reactome
  4. G1/S transition of mitotic cell cycle Source: Reactome
  5. 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 MCM5 (EC:3.6.4.12)
Alternative name(s):
CDC46 homolog
P1-CDC46
Gene namesi
Name:MCM5
Synonyms:CDC46
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:6948. MCM5.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30695.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 734733DNA replication licensing factor MCM5PRO_0000194107Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei392 – 3921N6-acetyllysine1 Publication
Modified residuei396 – 3961N6-acetyllysine1 Publication
Modified residuei696 – 6961N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP33992.
PaxDbiP33992.
PeptideAtlasiP33992.
PRIDEiP33992.

PTM databases

PhosphoSiteiP33992.

Miscellaneous databases

PMAP-CutDBP33992.

Expressioni

Gene expression databases

BgeeiP33992.
CleanExiHS_MCM5.
ExpressionAtlasiP33992. baseline and differential.
GenevestigatoriP33992.

Organism-specific databases

HPAiCAB000101.
HPA000845.
HPA052880.

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).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST2H4BP628052EBI-359410,EBI-302023
MCM2P497365EBI-359410,EBI-374819
MCM3P252054EBI-359410,EBI-355153
MCM7P339938EBI-359410,EBI-355924
MCMBPQ9BTE313EBI-359410,EBI-749378

Protein-protein interaction databases

BioGridi110342. 58 interactions.
DIPiDIP-27578N.
IntActiP33992. 40 interactions.
MINTiMINT-5004198.
STRINGi9606.ENSP00000216122.

Structurei

3D structure databases

ProteinModelPortaliP33992.
SMRiP33992. Positions 35-646.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini331 – 537207MCMAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1241.
GeneTreeiENSGT00550000074928.
HOGENOMiHOG000224128.
HOVERGENiHBG104907.
InParanoidiP33992.
KOiK02209.
OMAiIVKDTHD.
OrthoDBiEOG7SV0TR.
PhylomeDBiP33992.
TreeFamiTF105653.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR008048. MCM5.
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.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01661. MCMPROTEIN5.
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.

P33992-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGFDDPGIF YSDSFGGDAQ ADEGQARKSQ LQRRFKEFLR QYRVGTDRTG
60 70 80 90 100
FTFKYRDELK RHYNLGEYWI EVEMEDLASF DEDLADYLYK QPAEHLQLLE
110 120 130 140 150
EAAKEVADEV TRPRPSGEEV LQDIQVMLKS DASPSSIRSL KSDMMSHLVK
160 170 180 190 200
IPGIIIAASA VRAKATRISI QCRSCRNTLT NIAMRPGLEG YALPRKCNTD
210 220 230 240 250
QAGRPKCPLD PYFIMPDKCK CVDFQTLKLQ ELPDAVPHGE MPRHMQLYCD
260 270 280 290 300
RYLCDKVVPG NRVTIMGIYS IKKFGLTTSR GRDRVGVGIR SSYIRVLGIQ
310 320 330 340 350
VDTDGSGRSF AGAVSPQEEE EFRRLAALPN VYEVISKSIA PSIFGGTDMK
360 370 380 390 400
KAIACLLFGG SRKRLPDGLT RRGDINLLML GDPGTAKSQL LKFVEKCSPI
410 420 430 440 450
GVYTSGKGSS AAGLTASVMR DPSSRNFIME GGAMVLADGG VVCIDEFDKM
460 470 480 490 500
REDDRVAIHE AMEQQTISIA KAGITTTLNS RCSVLAAANS VFGRWDETKG
510 520 530 540 550
EDNIDFMPTI LSRFDMIFIV KDEHNEERDV MLAKHVITLH VSALTQTQAV
560 570 580 590 600
EGEIDLAKLK KFIAYCRVKC GPRLSAEAAE KLKNRYIIMR SGARQHERDS
610 620 630 640 650
DRRSSIPITV RQLEAIVRIA EALSKMKLQP FATEADVEEA LRLFQVSTLD
660 670 680 690 700
AALSGTLSGV EGFTSQEDQE MLSRIEKQLK RRFAIGSQVS EHSIIKDFTK
710 720 730
QKYPEHAIHK VLQLMLRRGE IQHRMQRKVL YRLK
Length:734
Mass (Da):82,286
Last modified:August 14, 2001 - v5
Checksum:iA80280E61749998D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411Q → R in AAH03656. (PubMed:15489334)Curated
Sequence conflicti434 – 4341M → W(PubMed:8265339)Curated
Sequence conflicti527 – 5271E → V in BAA12176. 1 PublicationCurated
Sequence conflicti591 – 5911S → T in BAA12176. 1 PublicationCurated
Sequence conflicti593 – 60311ARQHERDSDRR → PVSTRGTVTA in BAA12176. 1 PublicationCuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti136 – 1361S → T.1 Publication
Corresponds to variant rs2307334 [ dbSNP | Ensembl ].
VAR_014813
Natural varianti180 – 1801T → S.1 Publication
Corresponds to variant rs2307340 [ dbSNP | Ensembl ].
VAR_014814
Natural varianti258 – 2581V → I.1 Publication
Corresponds to variant rs2230933 [ dbSNP | Ensembl ].
VAR_014815

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74795 mRNA. Translation: CAA52802.2.
D83986 mRNA. Translation: BAA12176.1.
CR456517 mRNA. Translation: CAG30403.1.
AY212028 Genomic DNA. Translation: AAO21127.1.
Z82244 Genomic DNA. No translation available.
BC000142 mRNA. Translation: AAH00142.1.
BC003656 mRNA. Translation: AAH03656.1.
CCDSiCCDS13915.1.
PIRiI38080.
RefSeqiNP_006730.2. NM_006739.3.
UniGeneiHs.517582.

Genome annotation databases

EnsembliENST00000216122; ENSP00000216122; ENSG00000100297.
GeneIDi4174.
KEGGihsa:4174.
UCSCiuc003anu.4. human.

Polymorphism databases

DMDMi19858646.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74795 mRNA. Translation: CAA52802.2 .
D83986 mRNA. Translation: BAA12176.1 .
CR456517 mRNA. Translation: CAG30403.1 .
AY212028 Genomic DNA. Translation: AAO21127.1 .
Z82244 Genomic DNA. No translation available.
BC000142 mRNA. Translation: AAH00142.1 .
BC003656 mRNA. Translation: AAH03656.1 .
CCDSi CCDS13915.1.
PIRi I38080.
RefSeqi NP_006730.2. NM_006739.3.
UniGenei Hs.517582.

3D structure databases

ProteinModelPortali P33992.
SMRi P33992. Positions 35-646.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110342. 58 interactions.
DIPi DIP-27578N.
IntActi P33992. 40 interactions.
MINTi MINT-5004198.
STRINGi 9606.ENSP00000216122.

PTM databases

PhosphoSitei P33992.

Polymorphism databases

DMDMi 19858646.

Proteomic databases

MaxQBi P33992.
PaxDbi P33992.
PeptideAtlasi P33992.
PRIDEi P33992.

Protocols and materials databases

DNASUi 4174.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216122 ; ENSP00000216122 ; ENSG00000100297 .
GeneIDi 4174.
KEGGi hsa:4174.
UCSCi uc003anu.4. human.

Organism-specific databases

CTDi 4174.
GeneCardsi GC22P035798.
HGNCi HGNC:6948. MCM5.
HPAi CAB000101.
HPA000845.
HPA052880.
MIMi 602696. gene.
neXtProti NX_P33992.
PharmGKBi PA30695.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1241.
GeneTreei ENSGT00550000074928.
HOGENOMi HOG000224128.
HOVERGENi HBG104907.
InParanoidi P33992.
KOi K02209.
OMAi IVKDTHD.
OrthoDBi EOG7SV0TR.
PhylomeDBi P33992.
TreeFami TF105653.

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 MCM5. human.
GeneWikii MCM5.
GenomeRNAii 4174.
NextBioi 16442.
PMAP-CutDB P33992.
PROi P33992.
SOURCEi Search...

Gene expression databases

Bgeei P33992.
CleanExi HS_MCM5.
ExpressionAtlasi P33992. baseline and differential.
Genevestigatori P33992.

Family and domain databases

Gene3Di 2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProi IPR008048. MCM5.
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.
PF14551. MCM_N. 1 hit.
[Graphical view ]
PRINTSi PR01657. MCMFAMILY.
PR01661. MCMPROTEIN5.
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

« Hide 'large scale' publications
  1. Hu B.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cervix carcinoma.
  2. Goehring F., Jehnichen P., Hemmer W.H.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Homo sapiens DNA replication licensing factor (huMCM5)."
    Mimura S., Nishimoto S., Kubota Y., Takisawa H., Nojima H.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. NIEHS SNPs program
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-136; SER-180 AND ILE-258.
  6. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Lymph and Placenta.
  8. "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 352-590.
    Tissue: Cervix.
  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: INTERACTION WITH MCMBP, IDENTIFICATION IN THE MCM2-7 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "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-392; LYS-396 AND LYS-696, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCM5_HUMAN
AccessioniPrimary (citable) accession number: P33992
Secondary accession number(s): O60785
, Q14578, Q9BTJ4, Q9BWL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 14, 2001
Last modified: October 29, 2014
This is version 160 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. The MCM2-7 hexamer is the proposed physiological active complex.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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