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Protein
Submitted name:

DNA replication licensing factor MCM5

Gene

MCM5

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

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

GO - Biological processi

  1. DNA replication initiation Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
DNA replication licensing factor MCM5Imported
Gene namesi
Name:MCM5Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:6948. MCM5.

Subcellular locationi

GO - Cellular componenti

  1. MCM complex Source: InterPro
  2. nucleus Source: InterPro
Complete GO annotation...

PTM / Processingi

Proteomic databases

MaxQBiB1AHA9.
PRIDEiB1AHA9.

Expressioni

Gene expression databases

ExpressionAtlasiB1AHA9. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliB1AHA9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00550000074928.
HOGENOMiHOG000172515.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR008048. MCM5.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01661. MCMPROTEIN5.
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Fragment.

B1AHA9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGFDDPGIF YSDSFGGDAQ ADEGQARKSQ LQRRFKEFLR QYRVGTDRTG
60 70 80 90 100
FTFKYSLAPS LIEHLLPARY CSGCWAAALK LDLAPASRDE LKRHYNLGEY
110 120 130 140 150
WIEVEMEDLA SFDEDLADYL YKQPAEHLQL LEEAAKEVAD EVTRPRPSGE
160 170 180 190 200
EVLQDIQVML KSDASPSSIR SLKSDMMSHL VKIPGIIIAA SAVRAKATRI
210 220 230
SIQCRSCRNT LTNIAMRPGL EGYALPRKCN
Length:230
Mass (Da):25,843
Last modified:February 4, 2015 - v4
Checksum:i6803D7DC254F6DAE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei230 – 2301Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z82244 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000416905; ENSP00000393977; ENSG00000100297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z82244 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliB1AHA9.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

MaxQBiB1AHA9.
PRIDEiB1AHA9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000416905; ENSP00000393977; ENSG00000100297.

Organism-specific databases

HGNCiHGNC:6948. MCM5.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00550000074928.
HOGENOMiHOG000172515.

Miscellaneous databases

ChiTaRSiMCM5. human.
NextBioi35466375.

Gene expression databases

ExpressionAtlasiB1AHA9. baseline and differential.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR008048. MCM5.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01661. MCMPROTEIN5.
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiB1AHA9_HUMAN
AccessioniPrimary (citable) accession number: B1AHA9
Entry historyi
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: February 4, 2015
Last modified: February 4, 2015
This is version 48 of the entry and version 4 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.