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Q14692

- BMS1_HUMAN

UniProt

Q14692 - BMS1_HUMAN

Protein

Ribosome biogenesis protein BMS1 homolog

Gene

BMS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi89 – 968ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. ribosome assembly Source: UniProtKB

    Keywords - Biological processi

    Ribosome biogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosome biogenesis protein BMS1 homolog
    Alternative name(s):
    Ribosome assembly protein BMS1 homolog
    Gene namesi
    Name:BMS1
    Synonyms:BMS1L, KIAA0187
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:23505. BMS1.

    Subcellular locationi

    Nucleusnucleolus By similarity

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti1114. Circumscribed cutaneous aplasia of the vertex.
    PharmGKBiPA162377556.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12821282Ribosome biogenesis protein BMS1 homologPRO_0000195004Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei552 – 5521Phosphoserine2 Publications
    Modified residuei625 – 6251Phosphoserine1 Publication
    Modified residuei639 – 6391Phosphoserine1 Publication
    Modified residuei708 – 7081Phosphothreonine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ14692.
    PaxDbiQ14692.
    PeptideAtlasiQ14692.
    PRIDEiQ14692.

    PTM databases

    PhosphoSiteiQ14692.

    Expressioni

    Gene expression databases

    BgeeiQ14692.
    CleanExiHS_BMS1.
    GenevestigatoriQ14692.

    Organism-specific databases

    HPAiHPA036589.
    HPA043081.

    Interactioni

    Protein-protein interaction databases

    BioGridi115134. 9 interactions.
    IntActiQ14692. 6 interactions.
    MINTiMINT-3030112.
    STRINGi9606.ENSP00000363642.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14692.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 246167Bms1-type GAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5192.
    HOGENOMiHOG000166882.
    HOVERGENiHBG023890.
    InParanoidiQ14692.
    KOiK14569.
    OMAiPMVDRTP.
    OrthoDBiEOG7FNC7S.
    PhylomeDBiQ14692.
    TreeFamiTF105751.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    InterProiIPR012948. AARP2CN.
    IPR007034. BMS1_TSR1_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF08142. AARP2CN. 1 hit.
    PF04950. DUF663. 1 hit.
    [Graphical view]
    SMARTiSM00785. AARP2CN. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS51714. G_BMS1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q14692-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAKDQKKHR KKNSGPKAAK KKKRLLQDLQ LGDEEDARKR NPKAFAVQSA     50
    VRMARSFHRT QDLKTKKHHI PVVDRTPLEP PPIVVVVMGP PKVGKSTLIQ 100
    CLIRNFTRQK LTEIRGPVTI VSGKKRRLTI IECGCDINMM IDLAKVADLV 150
    LMLIDASFGF EMETFEFLNI CQVHGFPKIM GVLTHLDSFK HNKQLKKTKK 200
    RLKHRFWTEV YPGAKLFYLS GMVHGEYQNQ EIHNLGRFIT VMKFRPLTWQ 250
    TSHPYILADR MEDLTNPEDI RTNIKCDRKV SLYGYLRGAH LKNKSQIHMP 300
    GVGDFAVSDI SFLPDPCALP EQQKKRCLNE KEKLVYAPLS GVGGVLYDKD 350
    AVYVDLGGSH VFQDEVGPTH ELVQSLISTH STIDAKMASS RVTLFSDSKP 400
    LGSEDIDNQG LMMPKEEKQM DLNTGRMRRK AIFGDEDESG DSDDEEDDEM 450
    SEDDGLENGS SDEEAEEEEN AEMTDQYMAV KGIKRRKLEL EEDSEMDLPA 500
    FADSDDDLER SSAEEGEAEE ADESSEEEDC TAGEKGISGS KAAGEGSKAG 550
    LSPANCQSDR VNLEKSLLMK KAALPTFDSG HCTAEEVFAS EDESEESSSL 600
    SAEEEDSENE EAIRKKLSKP SQVSSGQKLG PQNFIDETSD IENLLKEEED 650
    YKEENNDSKE TSGALKWKED LSRKAAEAFL RQQQAAPNLR KLIYGTVTED 700
    NEEEDDDTLE ELGGLFRVNQ PDRECKHKAD SLDCSRFLVE APHDWDLEEV 750
    MNSIRDCFVT GKWEDDKDAA KVLAEDEELY GDFEDLETGD VHKGKSGPNT 800
    QNEDIEKEVK EEIDPDEEES AKKKHLDKKR KLKEMFDAEY DEGESTYFDD 850
    LKGEMQKQAQ LNRAEFEDQD DEARVQYEGF RPGMYVRIEI ENVPCEFVQN 900
    FDPHYPIILG GLGNSEGNVG YVQMRLKKHR WYKKILKSRD PIIFSVGWRR 950
    FQTIPLYYIE DHNGRQRLLK YTPQHMHCGA AFWGPITPQG TGFLAIQSVS 1000
    GIMPDFRIAA TGVVLDLDKS IKIVKKLKLT GFPYKIFKNT SFIKGMFNSA 1050
    LEVAKFEGAV IRTVSGIRGQ IKKALRAPEG AFRASFEDKL LMSDIVFMRT 1100
    WYPVSIPAFY NPVTSLLKPV GEKDTWSGMR TTGQLRLAHG VRLKANKDSL 1150
    YKPILRQKKH FNSLHIPKAL QKALPFKNKP KTQAKAGKVP KDRRRPAVIR 1200
    EPHERKILAL LDALSTVHSQ KMKKAKEQRH LHNKEHFRAK QKEEEEKLKR 1250
    QKDLRKKLFR IQGQKERRNQ KSSLKGAEGQ LQ 1282
    Length:1,282
    Mass (Da):145,807
    Last modified:November 1, 1996 - v1
    Checksum:i54A736ED250A5138
    GO

    Sequence cautioni

    The sequence BAA11504.2 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti237 – 2371R → H.
    Corresponds to variant rs2272881 [ dbSNP | Ensembl ].
    VAR_057503
    Natural varianti552 – 5521S → P.
    Corresponds to variant rs3814621 [ dbSNP | Ensembl ].
    VAR_057504
    Natural varianti652 – 6521K → R.
    Corresponds to variant rs787795 [ dbSNP | Ensembl ].
    VAR_057505
    Natural varianti884 – 8841M → V.
    Corresponds to variant rs2419109 [ dbSNP | Ensembl ].
    VAR_057506
    Natural varianti1141 – 11411V → I.1 Publication
    Corresponds to variant rs12764004 [ dbSNP | Ensembl ].
    VAR_057507

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D80009 mRNA. Translation: BAA11504.2. Different initiation.
    AL022344 Genomic DNA. Translation: CAI23617.1.
    CH471160 Genomic DNA. Translation: EAW86571.1.
    BC043345 mRNA. Translation: AAH43345.1.
    BC150252 mRNA. Translation: AAI50253.1.
    CCDSiCCDS7199.1.
    RefSeqiNP_055568.3. NM_014753.3.
    XP_005271903.1. XM_005271846.1.
    UniGeneiHs.10848.

    Genome annotation databases

    EnsembliENST00000374518; ENSP00000363642; ENSG00000165733.
    GeneIDi9790.
    KEGGihsa:9790.
    UCSCiuc001jaj.3. human.

    Polymorphism databases

    DMDMi27151474.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D80009 mRNA. Translation: BAA11504.2 . Different initiation.
    AL022344 Genomic DNA. Translation: CAI23617.1 .
    CH471160 Genomic DNA. Translation: EAW86571.1 .
    BC043345 mRNA. Translation: AAH43345.1 .
    BC150252 mRNA. Translation: AAI50253.1 .
    CCDSi CCDS7199.1.
    RefSeqi NP_055568.3. NM_014753.3.
    XP_005271903.1. XM_005271846.1.
    UniGenei Hs.10848.

    3D structure databases

    ProteinModelPortali Q14692.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115134. 9 interactions.
    IntActi Q14692. 6 interactions.
    MINTi MINT-3030112.
    STRINGi 9606.ENSP00000363642.

    PTM databases

    PhosphoSitei Q14692.

    Polymorphism databases

    DMDMi 27151474.

    Proteomic databases

    MaxQBi Q14692.
    PaxDbi Q14692.
    PeptideAtlasi Q14692.
    PRIDEi Q14692.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374518 ; ENSP00000363642 ; ENSG00000165733 .
    GeneIDi 9790.
    KEGGi hsa:9790.
    UCSCi uc001jaj.3. human.

    Organism-specific databases

    CTDi 9790.
    GeneCardsi GC10P043277.
    H-InvDB HIX0059462.
    HIX0172328.
    HIX0172329.
    HGNCi HGNC:23505. BMS1.
    HPAi HPA036589.
    HPA043081.
    MIMi 611448. gene.
    neXtProti NX_Q14692.
    Orphaneti 1114. Circumscribed cutaneous aplasia of the vertex.
    PharmGKBi PA162377556.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5192.
    HOGENOMi HOG000166882.
    HOVERGENi HBG023890.
    InParanoidi Q14692.
    KOi K14569.
    OMAi PMVDRTP.
    OrthoDBi EOG7FNC7S.
    PhylomeDBi Q14692.
    TreeFami TF105751.

    Miscellaneous databases

    ChiTaRSi BMS1. human.
    GenomeRNAii 9790.
    NextBioi 36866.
    PROi Q14692.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q14692.
    CleanExi HS_BMS1.
    Genevestigatori Q14692.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    InterProi IPR012948. AARP2CN.
    IPR007034. BMS1_TSR1_C.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF08142. AARP2CN. 1 hit.
    PF04950. DUF663. 1 hit.
    [Graphical view ]
    SMARTi SM00785. AARP2CN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS51714. G_BMS1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    2. "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].
    3. 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], VARIANT ILE-1141.
      Tissue: Skin.
    5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552; SER-625 AND THR-708, 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. "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-552 AND THR-708, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiBMS1_HUMAN
    AccessioniPrimary (citable) accession number: Q14692
    Secondary accession number(s): Q5QPT5, Q86XJ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 13, 2002
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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