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Q9BQG0

- MBB1A_HUMAN

UniProt

Q9BQG0 - MBB1A_HUMAN

Protein

Myb-binding protein 1A

Gene

MYBBP1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity) By similarity.By similarity

    GO - Molecular functioni

    1. DNA-directed DNA polymerase activity Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. sequence-specific DNA binding Source: Ensembl
    5. transcription factor binding Source: ProtInc

    GO - Biological processi

    1. cellular response to glucose starvation Source: UniProtKB
    2. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
    3. negative regulation of transcription, DNA-templated Source: Ensembl
    4. nucleocytoplasmic transport Source: UniProtKB
    5. osteoblast differentiation Source: UniProt
    6. positive regulation of cell cycle arrest Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: ProtInc
    8. respiratory electron transport chain Source: Ensembl
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myb-binding protein 1A
    Gene namesi
    Name:MYBBP1A
    Synonyms:P160
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7546. MYBBP1A.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. Nucleusnucleolus 1 Publication
    Note: Shuttles between the nucleus and cytoplasm. Nuclear import may be mediated by KPNA2, while export appears to depend partially on XPO1/CRM1 By similarity. Predominantly nucleolar.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. intracellular membrane-bounded organelle Source: HPA
    3. membrane Source: UniProtKB
    4. NLS-dependent protein nuclear import complex Source: UniProtKB
    5. nucleolus Source: UniProtKB
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31346.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13281328Myb-binding protein 1APRO_0000096255Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine5 Publications
    Modified residuei71 – 711N6-acetyllysine1 Publication
    Modified residuei158 – 1581N6-acetyllysine1 Publication
    Modified residuei775 – 7751Phosphoserine7 Publications
    Modified residuei1159 – 11591Phosphoserine1 Publication
    Modified residuei1163 – 11631Phosphoserine4 Publications
    Modified residuei1186 – 11861Phosphoserine2 Publications
    Modified residuei1190 – 11901Phosphothreonine1 Publication
    Modified residuei1196 – 11961Phosphothreonine1 Publication
    Modified residuei1207 – 12071Phosphoserine1 Publication
    Modified residuei1232 – 12321Phosphoserine1 Publication
    Modified residuei1241 – 12411PhosphoserineBy similarity
    Modified residuei1248 – 12481Phosphoserine1 Publication
    Modified residuei1267 – 12671Phosphoserine4 Publications
    Modified residuei1269 – 12691Phosphothreonine1 Publication
    Modified residuei1290 – 12901Phosphoserine3 Publications
    Modified residuei1303 – 13031Phosphoserine1 Publication
    Modified residuei1307 – 13071CitrullineBy similarity
    Modified residuei1308 – 13081Phosphoserine2 Publications
    Modified residuei1310 – 13101Phosphoserine1 Publication
    Modified residuei1314 – 13141Phosphoserine2 Publications

    Post-translational modificationi

    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BQG0.
    PaxDbiQ9BQG0.
    PRIDEiQ9BQG0.

    2D gel databases

    SWISS-2DPAGEQ9BQG0.

    PTM databases

    PhosphoSiteiQ9BQG0.

    Miscellaneous databases

    PMAP-CutDBQ9BQG0.

    Expressioni

    Gene expression databases

    BgeeiQ9BQG0.
    CleanExiHS_MYBBP1A.
    GenevestigatoriQ9BQG0.

    Organism-specific databases

    HPAiHPA005466.

    Interactioni

    Subunit structurei

    Binds to and represses JUN and MYB via the leucine zipper regions present in these proteins. Also binds to and represses PPARGC1A: this interaction is abrogated when PPARGC1A is phosphorylated by MAPK1/ERK. Binds to and stimulates transcription by AHR. Binds to KPNA2. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DHX30Q7L2E33EBI-676973,EBI-1211456
    NR2E3Q9Y5X42EBI-676973,EBI-7216962

    Protein-protein interaction databases

    BioGridi115770. 83 interactions.
    IntActiQ9BQG0. 29 interactions.
    MINTiMINT-1150245.
    STRINGi9606.ENSP00000370968.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BQG0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 582582Interaction with MYBBy similarityAdd
    BLAST
    Regioni1151 – 1328178Required for nuclear and nucleolar localizationBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi240 – 25819Nuclear export signal 1By similarityAdd
    BLAST
    Motifi263 – 28119Nuclear export signal 2By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi720 – 78465Glu-richAdd
    BLAST

    Phylogenomic databases

    eggNOGiNOG313877.
    HOGENOMiHOG000113488.
    HOVERGENiHBG081961.
    KOiK02331.
    OMAiHQAQACL.
    PhylomeDBiQ9BQG0.
    TreeFamiTF317401.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR007015. DNA_pol_V.
    [Graphical view]
    PANTHERiPTHR13213. PTHR13213. 1 hit.
    PfamiPF04931. DNA_pol_phi. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 5 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BQG0-1) [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

    MESRDPAQPM SPGEATQSGA RPADRYGLLK HSREFLDFFW DIAKPEQETR     50
    LAATEKLLEY LRGRPKGSEM KYALKRLITG LGVGRETARP CYSLALAQLL 100
    QSFEDLPLCS ILQQIQEKYD LHQVKKAMLR PALFANLFGV LALFQSGRLV 150
    KDQEALMKSV KLLQALAQYQ NHLQEQPRKA LVDILSEVSK ATLQEILPEV 200
    LKADLNIILS SPEQLELFLL AQQKVPSKLK KLVGSVNLFS DENVPRLVNV 250
    LKMAASSVKK DRKLPAIALD LLRLALKEDK FPRFWKEVVE QGLLKMQFWP 300
    ASYLCFRLLG AALPLLTKEQ LHLVMQGDVI RHYGEHVCTA KLPKQFKFAP 350
    EMDDYVGTFL EGCQDDPERQ LAVLVAFSSV TNQGLPVTPT FWRVVRFLSP 400
    PALQGYVAWL RAMFLQPDLD SLVDFSTNNQ KKAQDSSLHM PERAVFRLRK 450
    WIIFRLVSIV DSLHLEMEEA LTEQVARFCL FHSFFVTKKP TSQIPETKHP 500
    FSFPLENQAR EAVSSAFFSL LQTLSTQFKQ APGQTQGGQP WTYHLVQFAD 550
    LLLNHSHNVT TVTPFTAQQR QAWDRMLQTL KELEAHSAEA RAAAFQHLLL 600
    LVGIHLLKSP AESCDLLGDI QTCIRKSLGE KPRRSRTKTI DPQEPPWVEV 650
    LVEILLALLA QPSHLMRQVA RSVFGHICSH LTPRALQLIL DVLNPETSED 700
    ENDRVVVTDD SDERRLKGAE DKSEEGEDNR SSESEEESEG EESEEEERDG 750
    DVDQGFREQL MTVLQAGKAL GGEDSENEEE LGDEAMMALD QSLASLFAEQ 800
    KLRIQARRDE KNKLQKEKAL RRDFQIRVLD LVEVLVTKQP ENALVLELLE 850
    PLLSIIRRSL RSSSSKQEQD LLHKTARIFT HHLCRARRYC HDLGERAGAL 900
    HAQVERLVQQ AGRQPDSPTA LYHFNASLYL LRVLKGNTAE GCVHETQEKQ 950
    KAGTDPSHMP TGPQAASCLD LNLVTRVYST ALSSFLTKRN SPLTVPMFLS 1000
    LFSRHPVLCQ SLLPILVQHI TGPVRPRHQA CLLLQKTLSM REVRSCFEDP 1050
    EWKQLMGQVL AKVTENLRVL GEAQTKAQHQ QALSSLELLN VLFRTCKHEK 1100
    LTLDLTVLLG VLQGQQQSLQ QGAHSTGSSR LHDLYWQAMK TLGVQRPKLE 1150
    KKDAKEIPSA TQSPISKKRK KKGFLPETKK RKKRKSEDGT PAEDGTPAAT 1200
    GGSQPPSMGR KKRNRTKAKV PAQANGTPTT KSPAPGAPTR SPSTPAKSPK 1250
    LQKKNQKPSQ VNGAPGSPTE PAGQKQHQKA LPKKGVLGKS PLSALARKKA 1300
    RLSLVIRSPS LLQSGAKKKA QVRKAGKP 1328
    Length:1,328
    Mass (Da):148,855
    Last modified:July 19, 2005 - v2
    Checksum:i0B053465D5B3511F
    GO
    Isoform 2 (identifier: Q9BQG0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1322-1328: VRKAGKP → TLRFTISSSKK

    Note: May be due to competing donor and acceptor splice sites.

    Show »
    Length:1,332
    Mass (Da):149,367
    Checksum:iCF90678D49D64DB1
    GO

    Sequence cautioni

    The sequence CAB66530.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti307 – 3071R → H in AAF33021. (PubMed:10644447)Curated
    Sequence conflicti570 – 5701R → H in AAF33021. (PubMed:10644447)Curated
    Sequence conflicti601 – 6011L → F in AAF33021. (PubMed:10644447)Curated
    Sequence conflicti1028 – 10281H → R in AAH50546. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81Q → E.
    Corresponds to variant rs3809849 [ dbSNP | Ensembl ].
    VAR_023064
    Natural varianti680 – 6801H → Y.
    Corresponds to variant rs899440 [ dbSNP | Ensembl ].
    VAR_051156
    Natural varianti958 – 9581H → P.
    Corresponds to variant rs879797 [ dbSNP | Ensembl ].
    VAR_051157
    Natural varianti1208 – 12081M → L.
    Corresponds to variant rs9905742 [ dbSNP | Ensembl ].
    VAR_051158

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1322 – 13287VRKAGKP → TLRFTISSSKK in isoform 2. 1 PublicationVSP_014786

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF147709 mRNA. Translation: AAF33021.1.
    BC000641 mRNA. Translation: AAH00641.2.
    BC050546 mRNA. Translation: AAH50546.1.
    AL136595 mRNA. Translation: CAB66530.1. Different initiation.
    AL133098 mRNA. Translation: CAB61409.1.
    CCDSiCCDS11046.1. [Q9BQG0-1]
    CCDS42238.1. [Q9BQG0-2]
    PIRiT42680.
    RefSeqiNP_001099008.1. NM_001105538.1. [Q9BQG0-2]
    NP_055335.2. NM_014520.3. [Q9BQG0-1]
    UniGeneiHs.22824.
    Hs.701718.

    Genome annotation databases

    EnsembliENST00000254718; ENSP00000254718; ENSG00000132382. [Q9BQG0-1]
    ENST00000381556; ENSP00000370968; ENSG00000132382. [Q9BQG0-2]
    GeneIDi10514.
    KEGGihsa:10514.
    UCSCiuc002fxz.4. human. [Q9BQG0-2]
    uc002fyb.4. human. [Q9BQG0-1]

    Polymorphism databases

    DMDMi71153825.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF147709 mRNA. Translation: AAF33021.1 .
    BC000641 mRNA. Translation: AAH00641.2 .
    BC050546 mRNA. Translation: AAH50546.1 .
    AL136595 mRNA. Translation: CAB66530.1 . Different initiation.
    AL133098 mRNA. Translation: CAB61409.1 .
    CCDSi CCDS11046.1. [Q9BQG0-1 ]
    CCDS42238.1. [Q9BQG0-2 ]
    PIRi T42680.
    RefSeqi NP_001099008.1. NM_001105538.1. [Q9BQG0-2 ]
    NP_055335.2. NM_014520.3. [Q9BQG0-1 ]
    UniGenei Hs.22824.
    Hs.701718.

    3D structure databases

    ProteinModelPortali Q9BQG0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115770. 83 interactions.
    IntActi Q9BQG0. 29 interactions.
    MINTi MINT-1150245.
    STRINGi 9606.ENSP00000370968.

    PTM databases

    PhosphoSitei Q9BQG0.

    Polymorphism databases

    DMDMi 71153825.

    2D gel databases

    SWISS-2DPAGE Q9BQG0.

    Proteomic databases

    MaxQBi Q9BQG0.
    PaxDbi Q9BQG0.
    PRIDEi Q9BQG0.

    Protocols and materials databases

    DNASUi 10514.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254718 ; ENSP00000254718 ; ENSG00000132382 . [Q9BQG0-1 ]
    ENST00000381556 ; ENSP00000370968 ; ENSG00000132382 . [Q9BQG0-2 ]
    GeneIDi 10514.
    KEGGi hsa:10514.
    UCSCi uc002fxz.4. human. [Q9BQG0-2 ]
    uc002fyb.4. human. [Q9BQG0-1 ]

    Organism-specific databases

    CTDi 10514.
    GeneCardsi GC17M004442.
    H-InvDB HIX0013445.
    HGNCi HGNC:7546. MYBBP1A.
    HPAi HPA005466.
    MIMi 604885. gene.
    neXtProti NX_Q9BQG0.
    PharmGKBi PA31346.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313877.
    HOGENOMi HOG000113488.
    HOVERGENi HBG081961.
    KOi K02331.
    OMAi HQAQACL.
    PhylomeDBi Q9BQG0.
    TreeFami TF317401.

    Miscellaneous databases

    GeneWikii MYBBP1A.
    GenomeRNAii 10514.
    NextBioi 39876.
    PMAP-CutDB Q9BQG0.
    PROi Q9BQG0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BQG0.
    CleanExi HS_MYBBP1A.
    Genevestigatori Q9BQG0.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR007015. DNA_pol_V.
    [Graphical view ]
    PANTHERi PTHR13213. PTHR13213. 1 hit.
    Pfami PF04931. DNA_pol_phi. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 5 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and chromosomal mapping of the human homologue of MYB binding protein (P160) 1A (MYBBP1A) to 17p13.3."
      Keough R., Woollatt E., Crawford J., Sutherland G.R., Plummer S., Casey G., Gonda T.J.
      Genomics 62:483-489(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "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 1).
      Tissue: Eye.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-1328 (ISOFORM 2).
      Tissue: Amygdala.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 875-1328 (ISOFORM 1).
      Tissue: Testis.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "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-11 AND SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
      Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
      J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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-11; SER-775 AND SER-1290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-775; SER-1159; SER-1163; SER-1186; THR-1190; THR-1196; SER-1207; SER-1248; SER-1267; SER-1303; SER-1308 AND SER-1314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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].
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-775 AND SER-1267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-71 AND LYS-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-11; SER-775; SER-1163; SER-1267; SER-1290; SER-1308; SER-1310 AND SER-1314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-775; SER-1163; SER-1232; SER-1267; THR-1269 AND SER-1290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMBB1A_HUMAN
    AccessioniPrimary (citable) accession number: Q9BQG0
    Secondary accession number(s): Q86VM3
    , Q9BW49, Q9P0V5, Q9UF99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 120 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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

    External Data

    Dasty 3