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Q9BTE3

- MCMBP_HUMAN

UniProt

Q9BTE3 - MCMBP_HUMAN

Protein

Mini-chromosome maintenance complex-binding protein

Gene

MCMBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion.2 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. DNA-dependent DNA replication Source: UniProtKB
    2. mitotic nuclear division Source: UniProtKB-KW
    3. mitotic S phase Source: UniProtKB
    4. sister chromatid cohesion Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, DNA replication, Mitosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mini-chromosome maintenance complex-binding protein
    Short name:
    MCM-BP
    Short name:
    MCM-binding protein
    Gene namesi
    Name:MCMBP
    Synonyms:C10orf119
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:25782. MCMBP.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Associates with chromatin. Highly associated with chromatin in G1/S and S phases, reduced binding to chromatin in G2, and further decreased binding in early M phase. It then reassociates with chromatin in late M phase. Dissociates from chromatin later than component of the MCM complex.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: UniProtKB
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134862625.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 642642Mini-chromosome maintenance complex-binding proteinPRO_0000089827Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei154 – 1541Phosphoserine3 Publications
    Modified residuei160 – 1601Phosphothreonine1 Publication
    Modified residuei298 – 2981Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BTE3.
    PaxDbiQ9BTE3.
    PRIDEiQ9BTE3.

    PTM databases

    PhosphoSiteiQ9BTE3.

    Expressioni

    Gene expression databases

    BgeeiQ9BTE3.
    CleanExiHS_C10orf119.
    GenevestigatoriQ9BTE3.

    Organism-specific databases

    HPAiCAB013792.
    HPA038481.

    Interactioni

    Subunit structurei

    Interacts with the MCM complex: associates with the MCM3-7 complex which lacks MCM2, while it does not interact with the MCM complex when MCM2 is present (MCM2-7 complex). Interacts with the RPA complex, when composed of all RPA1, RPA2 and RPA3 components, but not with RPA1 or RPA2 alone.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC7O003112EBI-749378,EBI-374980
    GINS2Q9Y2482EBI-749378,EBI-747491
    GINS4Q9BRT92EBI-749378,EBI-747500
    MCM2P497364EBI-749378,EBI-374819
    MCM3P2520511EBI-749378,EBI-355153
    MCM4P3399114EBI-749378,EBI-374938
    MCM5P3399213EBI-749378,EBI-359410
    MCM6Q1456615EBI-749378,EBI-374900
    MCM7P3399316EBI-749378,EBI-355924
    MCM8Q9UJA33EBI-749378,EBI-8756095
    SMC3Q9UQE76EBI-749378,EBI-80718

    Protein-protein interaction databases

    BioGridi122976. 13 interactions.
    IntActiQ9BTE3. 20 interactions.
    MINTiMINT-1465513.
    STRINGi9606.ENSP00000353098.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4KG9X-ray1.70B152-161[»]
    ProteinModelPortaliQ9BTE3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MCMBP family.Curated

    Phylogenomic databases

    eggNOGiNOG325575.
    HOGENOMiHOG000237536.
    HOVERGENiHBG059839.
    InParanoidiQ9BTE3.
    OMAiLPSDCQV.
    OrthoDBiEOG7F511C.
    PhylomeDBiQ9BTE3.
    TreeFamiTF324793.

    Family and domain databases

    InterProiIPR019140. MCM_complex-bd.
    [Graphical view]
    PANTHERiPTHR13489. PTHR13489. 1 hit.
    PfamiPF09739. MCM_bind. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BTE3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPCGEDWLSH PLGIVQGFFA QNGVNPDWEK KVIEYFKEKL KENNAPKWVP    50
    SLNEVPLHYL KPNSFVKFRC MIQDMFDPEF YMGVYETVNQ NTKAHVLHFG 100
    KYRDVAECGP QQELDLNSPR NTTLERQTFY CVPVPGESTW VKEAYVNANQ 150
    ARVSPSTSYT PSRHKRSYED DDDMDLQPNK QKDQHAGARQ AGSVGGLQWC 200
    GEPKRLETEA STGQQLNSLN LSSPFDLNFP LPGEKGPACL VKVYEDWDCF 250
    KVNDILELYG ILSVDPVLSI LNNDERDASA LLDPMECTDT AEEQRVHSPP 300
    ASLVPRIHVI LAQKLQHINP LLPACLNKEE SKTCKFVSSF MSELSPVRAE 350
    LLGFLTHALL GDSLAAEYLI LHLISTVYTR RDVLPLGKFT VNLSGCPRNS 400
    TFTEHLYRII QHLVPASFRL QMTIENMNHL KFIPHKDYTA NRLVSGLLQL 450
    PSNTSLVIDE TLLEQGQLDT PGVHNVTALS NLITWQKVDY DFSYHQMEFP 500
    CNINVFITSE GRSLLPADCQ IHLQPQLIPP NMEEYMNSLL SAVLPSVLNK 550
    FRIYLTLLRF LEYSISDEIT KAVEDDFVEM RKNDPQSITA DDLHQLLVVA 600
    RCLSLSAGQT TLSRERWLRA KQLESLRRTR LQQQKCVNGN EL 642
    Length:642
    Mass (Da):72,980
    Last modified:July 19, 2005 - v2
    Checksum:iD9EA81646F1D50E2
    GO
    Isoform 2 (identifier: Q9BTE3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         334-335: Missing.

    Show »
    Length:640
    Mass (Da):72,749
    Checksum:iF7B4B5237F033E09
    GO
    Isoform 3 (identifier: Q9BTE3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-173: Missing.
         334-335: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:467
    Mass (Da):52,652
    Checksum:i723B4CAC74EC4791
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti164 – 1641H → Y in CAG33580. 1 PublicationCurated
    Sequence conflicti350 – 3501E → V in CAG33580. 1 PublicationCurated
    Sequence conflicti610 – 6101T → A in BAG52809. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 173173Missing in isoform 3. CuratedVSP_040721Add
    BLAST
    Alternative sequencei334 – 3352Missing in isoform 2 and isoform 3. 2 PublicationsVSP_014707

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK023143 mRNA. Translation: BAB14427.1.
    AK094075 mRNA. Translation: BAG52809.1.
    CR457299 mRNA. Translation: CAG33580.1.
    AC027672 Genomic DNA. No translation available.
    BC000935 mRNA. Translation: AAH00935.1.
    BC004183 mRNA. Translation: AAH04183.1.
    BC007219 mRNA. Translation: AAH07219.1.
    CCDSiCCDS58099.1. [Q9BTE3-2]
    CCDS7617.1. [Q9BTE3-1]
    RefSeqiNP_001243307.1. NM_001256378.1. [Q9BTE3-2]
    NP_001243308.1. NM_001256379.1. [Q9BTE3-3]
    NP_079110.1. NM_024834.3. [Q9BTE3-1]
    UniGeneiHs.124246.

    Genome annotation databases

    EnsembliENST00000360003; ENSP00000353098; ENSG00000197771. [Q9BTE3-1]
    ENST00000369077; ENSP00000358073; ENSG00000197771. [Q9BTE3-2]
    GeneIDi79892.
    KEGGihsa:79892.
    UCSCiuc001leq.2. human. [Q9BTE3-2]
    uc001ler.3. human. [Q9BTE3-1]
    uc001les.2. human. [Q9BTE3-3]

    Polymorphism databases

    DMDMi71153001.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK023143 mRNA. Translation: BAB14427.1 .
    AK094075 mRNA. Translation: BAG52809.1 .
    CR457299 mRNA. Translation: CAG33580.1 .
    AC027672 Genomic DNA. No translation available.
    BC000935 mRNA. Translation: AAH00935.1 .
    BC004183 mRNA. Translation: AAH04183.1 .
    BC007219 mRNA. Translation: AAH07219.1 .
    CCDSi CCDS58099.1. [Q9BTE3-2 ]
    CCDS7617.1. [Q9BTE3-1 ]
    RefSeqi NP_001243307.1. NM_001256378.1. [Q9BTE3-2 ]
    NP_001243308.1. NM_001256379.1. [Q9BTE3-3 ]
    NP_079110.1. NM_024834.3. [Q9BTE3-1 ]
    UniGenei Hs.124246.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4KG9 X-ray 1.70 B 152-161 [» ]
    ProteinModelPortali Q9BTE3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122976. 13 interactions.
    IntActi Q9BTE3. 20 interactions.
    MINTi MINT-1465513.
    STRINGi 9606.ENSP00000353098.

    PTM databases

    PhosphoSitei Q9BTE3.

    Polymorphism databases

    DMDMi 71153001.

    Proteomic databases

    MaxQBi Q9BTE3.
    PaxDbi Q9BTE3.
    PRIDEi Q9BTE3.

    Protocols and materials databases

    DNASUi 79892.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360003 ; ENSP00000353098 ; ENSG00000197771 . [Q9BTE3-1 ]
    ENST00000369077 ; ENSP00000358073 ; ENSG00000197771 . [Q9BTE3-2 ]
    GeneIDi 79892.
    KEGGi hsa:79892.
    UCSCi uc001leq.2. human. [Q9BTE3-2 ]
    uc001ler.3. human. [Q9BTE3-1 ]
    uc001les.2. human. [Q9BTE3-3 ]

    Organism-specific databases

    CTDi 79892.
    GeneCardsi GC10M121588.
    HGNCi HGNC:25782. MCMBP.
    HPAi CAB013792.
    HPA038481.
    MIMi 610909. gene.
    neXtProti NX_Q9BTE3.
    PharmGKBi PA134862625.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325575.
    HOGENOMi HOG000237536.
    HOVERGENi HBG059839.
    InParanoidi Q9BTE3.
    OMAi LPSDCQV.
    OrthoDBi EOG7F511C.
    PhylomeDBi Q9BTE3.
    TreeFami TF324793.

    Miscellaneous databases

    ChiTaRSi MCMBP. human.
    GenomeRNAii 79892.
    NextBioi 69714.
    PROi Q9BTE3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BTE3.
    CleanExi HS_C10orf119.
    Genevestigatori Q9BTE3.

    Family and domain databases

    InterProi IPR019140. MCM_complex-bd.
    [Graphical view ]
    PANTHERi PTHR13489. PTHR13489. 1 hit.
    Pfami PF09739. MCM_bind. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-642 (ISOFORMS 1/2).
      Tissue: Muscle and Placenta.
    5. "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: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE MCM COMPLEX.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; THR-160 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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].
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Identification of proteins that may directly interact with human RPA."
      Nakaya R., Takaya J., Onuki T., Moritani M., Nozaki N., Ishimi Y.
      J. Biochem. 148:539-547(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE RPA COMPLEX.
    10. "The MCM-binding protein ETG1 aids sister chromatid cohesion required for postreplicative homologous recombination repair."
      Takahashi N., Quimbaya M., Schubert V., Lammens T., Vandepoele K., Schubert I., Matsui M., Inze D., Berx G., De Veylder L.
      PLoS Genet. 6:E1000817-E1000817(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "MCM-BP regulates unloading of the MCM2-7 helicase in late S phase."
      Nishiyama A., Frappier L., Mechali M.
      Genes Dev. 25:165-175(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMCMBP_HUMAN
    AccessioniPrimary (citable) accession number: Q9BTE3
    Secondary accession number(s): B3KSP7
    , Q6IA56, Q9BVT9, Q9H916
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families
    5. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries

    External Data

    Dasty 3