MYBBP1A | ENSG00000132382 | NCBI 10514

Details for: MYBBP1A

Gene ID: 10514

Symbol: MYBBP1A

Ensembl ID: ENSG00000132382

Description: MYB binding protein 1a

Associated with

B-wich complex positively regulates rrna expression
(R-HSA-5250924)
Epigenetic regulation of gene expression
(R-HSA-212165)
Gene expression (transcription)
(R-HSA-74160)
Positive epigenetic regulation of rrna expression
(R-HSA-5250913)
B-wich complex
(GO:0110016)
Cellular response to glucose starvation
(GO:0042149)
Chromatin remodeling
(GO:0006338)
Circadian regulation of gene expression
(GO:0032922)
Cytoplasm
(GO:0005737)
E-box binding
(GO:0070888)
Intracellular membrane-bounded organelle
(GO:0043231)
Intrinsic apoptotic signaling pathway by p53 class mediator
(GO:0072332)
Membrane
(GO:0016020)
Negative regulation of dna-templated transcription
(GO:0045892)
Nls-dependent protein nuclear import complex
(GO:0042564)
Nucleolus
(GO:0005730)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Osteoblast differentiation
(GO:0001649)
Positive regulation of anoikis
(GO:2000210)
Positive regulation of transcription by rna polymerase i
(GO:0045943)
Positive regulation of transcription by rna polymerase ii
(GO:0045944)
Positive regulation of transcription by rna polymerase iii
(GO:0045945)
Regulation of dna-templated transcription
(GO:0006355)
Regulation of g1 to g0 transition
(GO:1903450)
Respiratory electron transport chain
(GO:0022904)
Ribosome biogenesis
(GO:0042254)
Rna binding
(GO:0003723)
Sequence-specific dna binding
(GO:0043565)
Transcription corepressor activity
(GO:0003714)

Other Information

Proteins

Myb-binding protein 1A

Genular Protein ID: 331663049

Symbol: MBB1A_HUMAN

Name: Myb-binding protein 1A

UniProtKB Accession Codes:

Q9BQG0 Q86VM3 Q9BW49 Q9P0V5 Q9UF99

Database IDs:

Citations:

PubMed ID: 10644447

Title: Molecular cloning and chromosomal mapping of the human homologue of MYB binding protein (P160) 1A (MYBBP1A) to 17p13.3.

PubMed ID: 10644447

DOI: 10.1006/geno.1999.6035

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11230166

Title: Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.

PubMed ID: 11230166

DOI: 10.1101/gr.gr1547r

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 12429849

Title: Functional proteomic analysis of human nucleolus.

PubMed ID: 12429849

DOI: 10.1091/mbc.e02-05-0271

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16603771

Title: The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription.

PubMed ID: 16603771

DOI: 10.1074/jbc.m600233200

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 29065309

Title: PWP1 Mediates Nutrient-Dependent Growth Control through Nucleolar Regulation of Ribosomal Gene Expression.

PubMed ID: 29065309

DOI: 10.1016/j.devcel.2017.09.022

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

Sequence Information:

Length: 1328
Mass: 148855
Checksum: 0B053465D5B3511F
Sequence:

MESRDPAQPM SPGEATQSGA RPADRYGLLK HSREFLDFFW DIAKPEQETR LAATEKLLEY 
LRGRPKGSEM KYALKRLITG LGVGRETARP CYSLALAQLL QSFEDLPLCS ILQQIQEKYD 
LHQVKKAMLR PALFANLFGV LALFQSGRLV KDQEALMKSV KLLQALAQYQ NHLQEQPRKA 
LVDILSEVSK ATLQEILPEV LKADLNIILS SPEQLELFLL AQQKVPSKLK KLVGSVNLFS 
DENVPRLVNV LKMAASSVKK DRKLPAIALD LLRLALKEDK FPRFWKEVVE QGLLKMQFWP 
ASYLCFRLLG AALPLLTKEQ LHLVMQGDVI RHYGEHVCTA KLPKQFKFAP EMDDYVGTFL 
EGCQDDPERQ LAVLVAFSSV TNQGLPVTPT FWRVVRFLSP PALQGYVAWL RAMFLQPDLD 
SLVDFSTNNQ KKAQDSSLHM PERAVFRLRK WIIFRLVSIV DSLHLEMEEA LTEQVARFCL 
FHSFFVTKKP TSQIPETKHP FSFPLENQAR EAVSSAFFSL LQTLSTQFKQ APGQTQGGQP 
WTYHLVQFAD LLLNHSHNVT TVTPFTAQQR QAWDRMLQTL KELEAHSAEA RAAAFQHLLL 
LVGIHLLKSP AESCDLLGDI QTCIRKSLGE KPRRSRTKTI DPQEPPWVEV LVEILLALLA 
QPSHLMRQVA RSVFGHICSH LTPRALQLIL DVLNPETSED ENDRVVVTDD SDERRLKGAE 
DKSEEGEDNR SSESEEESEG EESEEEERDG DVDQGFREQL MTVLQAGKAL GGEDSENEEE 
LGDEAMMALD QSLASLFAEQ KLRIQARRDE KNKLQKEKAL RRDFQIRVLD LVEVLVTKQP 
ENALVLELLE PLLSIIRRSL RSSSSKQEQD LLHKTARIFT HHLCRARRYC HDLGERAGAL 
HAQVERLVQQ AGRQPDSPTA LYHFNASLYL LRVLKGNTAE GCVHETQEKQ KAGTDPSHMP 
TGPQAASCLD LNLVTRVYST ALSSFLTKRN SPLTVPMFLS LFSRHPVLCQ SLLPILVQHI 
TGPVRPRHQA CLLLQKTLSM REVRSCFEDP EWKQLMGQVL AKVTENLRVL GEAQTKAQHQ 
QALSSLELLN VLFRTCKHEK LTLDLTVLLG VLQGQQQSLQ QGAHSTGSSR LHDLYWQAMK 
TLGVQRPKLE KKDAKEIPSA TQSPISKKRK KKGFLPETKK RKKRKSEDGT PAEDGTPAAT 
GGSQPPSMGR KKRNRTKAKV PAQANGTPTT KSPAPGAPTR SPSTPAKSPK LQKKNQKPSQ 
VNGAPGSPTE PAGQKQHQKA LPKKGVLGKS PLSALARKKA RLSLVIRSPS LLQSGAKKKA 
QVRKAGKP

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: MYBBP1A

Associated with

Other Information

Molecular cloning and chromosomal mapping of the human homologue of MYB binding protein (P160) 1A (MYBBP1A) to 17p13.3. PubMed ID: 10644447

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. PubMed ID: 11230166

The full-ORF clone resource of the German cDNA consortium. PubMed ID: 17974005

Functional proteomic analysis of human nucleolus. PubMed ID: 12429849

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription. PubMed ID: 16603771

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. PubMed ID: 18220336

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Large-scale proteomics analysis of the human kinome. PubMed ID: 19369195

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

PWP1 Mediates Nutrient-Dependent Growth Control through Nucleolar Regulation of Ribosomal Gene Expression. PubMed ID: 29065309

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733