Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myb-binding protein 1A

Gene

MYBBP1A

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

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). Acts as a corepressor and in concert with CRY1, represses the transcription of the core circadian clock component PER2. Preferentially binds to dimethylated histone H3 'Lys-9' (H3K9me2) on the PER2 promoter.By similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to glucose starvation Source: UniProtKB
  • circadian regulation of gene expression Source: UniProtKB
  • intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • nucleocytoplasmic transport Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • positive regulation of anoikis Source: CACAO
  • positive regulation of cell cycle arrest Source: UniProtKB
  • regulation of transcription, DNA-templated Source: ProtInc
  • respiratory electron transport chain Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, 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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:7546. MYBBP1A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • NLS-dependent protein nuclear import complex Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31346.

Polymorphism and mutation databases

BioMutaiMYBBP1A.
DMDMi71153825.

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.
ExpressionAtlasiQ9BQG0. baseline and differential.
GenevisibleiQ9BQG0. HS.

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. Interacts wih CLOCK and CRY1 (By similarity). Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21.By similarity1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi115770. 87 interactions.
IntActiQ9BQG0. 31 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.
GeneTreeiENSGT00390000017457.
HOGENOMiHOG000113488.
HOVERGENiHBG081961.
InParanoidiQ9BQG0.
KOiK02331.
OMAiPRIHSLW.
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. AlignAdd to basket

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

        10         20         30         40         50
MESRDPAQPM SPGEATQSGA RPADRYGLLK HSREFLDFFW DIAKPEQETR
60 70 80 90 100
LAATEKLLEY LRGRPKGSEM KYALKRLITG LGVGRETARP CYSLALAQLL
110 120 130 140 150
QSFEDLPLCS ILQQIQEKYD LHQVKKAMLR PALFANLFGV LALFQSGRLV
160 170 180 190 200
KDQEALMKSV KLLQALAQYQ NHLQEQPRKA LVDILSEVSK ATLQEILPEV
210 220 230 240 250
LKADLNIILS SPEQLELFLL AQQKVPSKLK KLVGSVNLFS DENVPRLVNV
260 270 280 290 300
LKMAASSVKK DRKLPAIALD LLRLALKEDK FPRFWKEVVE QGLLKMQFWP
310 320 330 340 350
ASYLCFRLLG AALPLLTKEQ LHLVMQGDVI RHYGEHVCTA KLPKQFKFAP
360 370 380 390 400
EMDDYVGTFL EGCQDDPERQ LAVLVAFSSV TNQGLPVTPT FWRVVRFLSP
410 420 430 440 450
PALQGYVAWL RAMFLQPDLD SLVDFSTNNQ KKAQDSSLHM PERAVFRLRK
460 470 480 490 500
WIIFRLVSIV DSLHLEMEEA LTEQVARFCL FHSFFVTKKP TSQIPETKHP
510 520 530 540 550
FSFPLENQAR EAVSSAFFSL LQTLSTQFKQ APGQTQGGQP WTYHLVQFAD
560 570 580 590 600
LLLNHSHNVT TVTPFTAQQR QAWDRMLQTL KELEAHSAEA RAAAFQHLLL
610 620 630 640 650
LVGIHLLKSP AESCDLLGDI QTCIRKSLGE KPRRSRTKTI DPQEPPWVEV
660 670 680 690 700
LVEILLALLA QPSHLMRQVA RSVFGHICSH LTPRALQLIL DVLNPETSED
710 720 730 740 750
ENDRVVVTDD SDERRLKGAE DKSEEGEDNR SSESEEESEG EESEEEERDG
760 770 780 790 800
DVDQGFREQL MTVLQAGKAL GGEDSENEEE LGDEAMMALD QSLASLFAEQ
810 820 830 840 850
KLRIQARRDE KNKLQKEKAL RRDFQIRVLD LVEVLVTKQP ENALVLELLE
860 870 880 890 900
PLLSIIRRSL RSSSSKQEQD LLHKTARIFT HHLCRARRYC HDLGERAGAL
910 920 930 940 950
HAQVERLVQQ AGRQPDSPTA LYHFNASLYL LRVLKGNTAE GCVHETQEKQ
960 970 980 990 1000
KAGTDPSHMP TGPQAASCLD LNLVTRVYST ALSSFLTKRN SPLTVPMFLS
1010 1020 1030 1040 1050
LFSRHPVLCQ SLLPILVQHI TGPVRPRHQA CLLLQKTLSM REVRSCFEDP
1060 1070 1080 1090 1100
EWKQLMGQVL AKVTENLRVL GEAQTKAQHQ QALSSLELLN VLFRTCKHEK
1110 1120 1130 1140 1150
LTLDLTVLLG VLQGQQQSLQ QGAHSTGSSR LHDLYWQAMK TLGVQRPKLE
1160 1170 1180 1190 1200
KKDAKEIPSA TQSPISKKRK KKGFLPETKK RKKRKSEDGT PAEDGTPAAT
1210 1220 1230 1240 1250
GGSQPPSMGR KKRNRTKAKV PAQANGTPTT KSPAPGAPTR SPSTPAKSPK
1260 1270 1280 1290 1300
LQKKNQKPSQ VNGAPGSPTE PAGQKQHQKA LPKKGVLGKS PLSALARKKA
1310 1320
RLSLVIRSPS LLQSGAKKKA QVRKAGKP
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. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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.
ENST00000381556; ENSP00000370968; ENSG00000132382. [Q9BQG0-2]
GeneIDi10514.
KEGGihsa:10514.
UCSCiuc002fxz.4. human. [Q9BQG0-2]
uc002fyb.4. human. [Q9BQG0-1]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9BQG0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115770. 87 interactions.
IntActiQ9BQG0. 31 interactions.
MINTiMINT-1150245.
STRINGi9606.ENSP00000370968.

PTM databases

PhosphoSiteiQ9BQG0.

Polymorphism and mutation databases

BioMutaiMYBBP1A.
DMDMi71153825.

2D gel databases

SWISS-2DPAGEQ9BQG0.

Proteomic databases

MaxQBiQ9BQG0.
PaxDbiQ9BQG0.
PRIDEiQ9BQG0.

Protocols and materials databases

DNASUi10514.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10514.
GeneCardsiGC17M004442.
H-InvDBHIX0013445.
HGNCiHGNC:7546. MYBBP1A.
HPAiHPA005466.
MIMi604885. gene.
neXtProtiNX_Q9BQG0.
PharmGKBiPA31346.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG313877.
GeneTreeiENSGT00390000017457.
HOGENOMiHOG000113488.
HOVERGENiHBG081961.
InParanoidiQ9BQG0.
KOiK02331.
OMAiPRIHSLW.
PhylomeDBiQ9BQG0.
TreeFamiTF317401.

Miscellaneous databases

ChiTaRSiMYBBP1A. human.
GeneWikiiMYBBP1A.
GenomeRNAii10514.
NextBioi39876.
PMAP-CutDBQ9BQG0.
PROiQ9BQG0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BQG0.
CleanExiHS_MYBBP1A.
ExpressionAtlasiQ9BQG0. baseline and differential.
GenevisibleiQ9BQG0. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 129 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

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.