Q9BQG0 (MBB1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myb-binding protein 1A

Gene names

Name:	MYBBP1A
Synonyms:	P160

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1328 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.7
Subcellular location	Cytoplasm. Nucleus. Nucleus › nucleolus. 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. Ref.5
Sequence caution	The sequence CAB66530.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Activator Repressor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to glucose starvation Inferred from direct assay PubMed 21471221. Source: UniProtKB intrinsic apoptotic signaling pathway by p53 class mediator Inferred from mutant phenotype PubMed 21471221. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara nucleocytoplasmic transport Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell cycle arrest Inferred from mutant phenotype PubMed 21471221. Source: UniProtKB regulation of transcription, DNA-dependent Traceable author statement Ref.1. Source: ProtInc respiratory electron transport chain Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	NLS-dependent protein nuclear import complex Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from direct assay PubMed 21471221. Source: UniProtKB
Molecular_function	DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding Inferred from electronic annotation. Source: Compara transcription factor binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BQG0-1)

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.

Isoform 2 (identifier: Q9BQG0-2)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1328	1328	Myb-binding protein 1A		PRO_0000096255
Regions
	Region	1 – 582	582	Interaction with MYB By similarity
	Region	1151 – 1328	178	Required for nuclear and nucleolar localization By similarity
	Motif	240 – 258	19	Nuclear export signal 1 By similarity
	Motif	263 – 281	19	Nuclear export signal 2 By similarity
	Compositional bias	720 – 784	65	Glu-rich
Amino acid modifications
	Modified residue	11	1	Phosphoserine Ref.6 Ref.8 Ref.10 Ref.11 Ref.15
	Modified residue	71	1	N6-acetyllysine Ref.14
	Modified residue	158	1	N6-acetyllysine Ref.14
	Modified residue	775	1	Phosphoserine Ref.6 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17
	Modified residue	1159	1	Phosphoserine Ref.11
	Modified residue	1163	1	Phosphoserine Ref.8 Ref.11 Ref.15 Ref.17
	Modified residue	1186	1	Phosphoserine Ref.9 Ref.11
	Modified residue	1190	1	Phosphothreonine Ref.11
	Modified residue	1196	1	Phosphothreonine Ref.11
	Modified residue	1207	1	Phosphoserine Ref.11
	Modified residue	1232	1	Phosphoserine Ref.17
	Modified residue	1241	1	Phosphoserine By similarity
	Modified residue	1248	1	Phosphoserine Ref.11
	Modified residue	1267	1	Phosphoserine Ref.11 Ref.13 Ref.15 Ref.17
	Modified residue	1269	1	Phosphothreonine Ref.17
	Modified residue	1290	1	Phosphoserine Ref.10 Ref.15 Ref.17
	Modified residue	1303	1	Phosphoserine Ref.11
	Modified residue	1308	1	Phosphoserine Ref.11 Ref.15
	Modified residue	1310	1	Phosphoserine Ref.15
	Modified residue	1314	1	Phosphoserine Ref.11 Ref.15
Natural variations
	Alternative sequence	1322 – 1328	7	VRKAGKP → TLRFTISSSKK in isoform 2.		VSP_014786
	Natural variant	8	1	Q → E. Corresponds to variant rs3809849 [ dbSNP | Ensembl ].		VAR_023064
	Natural variant	680	1	H → Y. Corresponds to variant rs899440 [ dbSNP | Ensembl ].		VAR_051156
	Natural variant	958	1	H → P. Corresponds to variant rs879797 [ dbSNP | Ensembl ].		VAR_051157
	Natural variant	1208	1	M → L. Corresponds to variant rs9905742 [ dbSNP | Ensembl ].		VAR_051158
Experimental info
	Sequence conflict	307	1	R → H in AAF33021. Ref.1
	Sequence conflict	570	1	R → H in AAF33021. Ref.1
	Sequence conflict	601	1	L → F in AAF33021. Ref.1
	Sequence conflict	1028	1	H → R in AAH50546. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2005. Version 2. Checksum: 0B053465D5B3511F	FASTA	1,328	148,855
	10 20 30 40 50 60 MESRDPAQPM SPGEATQSGA RPADRYGLLK HSREFLDFFW DIAKPEQETR LAATEKLLEY 70 80 90 100 110 120 LRGRPKGSEM KYALKRLITG LGVGRETARP CYSLALAQLL QSFEDLPLCS ILQQIQEKYD 130 140 150 160 170 180 LHQVKKAMLR PALFANLFGV LALFQSGRLV KDQEALMKSV KLLQALAQYQ NHLQEQPRKA 190 200 210 220 230 240 LVDILSEVSK ATLQEILPEV LKADLNIILS SPEQLELFLL AQQKVPSKLK KLVGSVNLFS 250 260 270 280 290 300 DENVPRLVNV LKMAASSVKK DRKLPAIALD LLRLALKEDK FPRFWKEVVE QGLLKMQFWP 310 320 330 340 350 360 ASYLCFRLLG AALPLLTKEQ LHLVMQGDVI RHYGEHVCTA KLPKQFKFAP EMDDYVGTFL 370 380 390 400 410 420 EGCQDDPERQ LAVLVAFSSV TNQGLPVTPT FWRVVRFLSP PALQGYVAWL RAMFLQPDLD 430 440 450 460 470 480 SLVDFSTNNQ KKAQDSSLHM PERAVFRLRK WIIFRLVSIV DSLHLEMEEA LTEQVARFCL 490 500 510 520 530 540 FHSFFVTKKP TSQIPETKHP FSFPLENQAR EAVSSAFFSL LQTLSTQFKQ APGQTQGGQP 550 560 570 580 590 600 WTYHLVQFAD LLLNHSHNVT TVTPFTAQQR QAWDRMLQTL KELEAHSAEA RAAAFQHLLL 610 620 630 640 650 660 LVGIHLLKSP AESCDLLGDI QTCIRKSLGE KPRRSRTKTI DPQEPPWVEV LVEILLALLA 670 680 690 700 710 720 QPSHLMRQVA RSVFGHICSH LTPRALQLIL DVLNPETSED ENDRVVVTDD SDERRLKGAE 730 740 750 760 770 780 DKSEEGEDNR SSESEEESEG EESEEEERDG DVDQGFREQL MTVLQAGKAL GGEDSENEEE 790 800 810 820 830 840 LGDEAMMALD QSLASLFAEQ KLRIQARRDE KNKLQKEKAL RRDFQIRVLD LVEVLVTKQP 850 860 870 880 890 900 ENALVLELLE PLLSIIRRSL RSSSSKQEQD LLHKTARIFT HHLCRARRYC HDLGERAGAL 910 920 930 940 950 960 HAQVERLVQQ AGRQPDSPTA LYHFNASLYL LRVLKGNTAE GCVHETQEKQ KAGTDPSHMP 970 980 990 1000 1010 1020 TGPQAASCLD LNLVTRVYST ALSSFLTKRN SPLTVPMFLS LFSRHPVLCQ SLLPILVQHI 1030 1040 1050 1060 1070 1080 TGPVRPRHQA CLLLQKTLSM REVRSCFEDP EWKQLMGQVL AKVTENLRVL GEAQTKAQHQ 1090 1100 1110 1120 1130 1140 QALSSLELLN VLFRTCKHEK LTLDLTVLLG VLQGQQQSLQ QGAHSTGSSR LHDLYWQAMK 1150 1160 1170 1180 1190 1200 TLGVQRPKLE KKDAKEIPSA TQSPISKKRK KKGFLPETKK RKKRKSEDGT PAEDGTPAAT 1210 1220 1230 1240 1250 1260 GGSQPPSMGR KKRNRTKAKV PAQANGTPTT KSPAPGAPTR SPSTPAKSPK LQKKNQKPSQ 1270 1280 1290 1300 1310 1320 VNGAPGSPTE PAGQKQHQKA LPKKGVLGKS PLSALARKKA RLSLVIRSPS LLQSGAKKKA QVRKAGKP
	Isoform 2 [UniParc]. Checksum: CF90678D49D64DB1	FASTA	1,332	149,367
	10 20 30 40 50 60 MESRDPAQPM SPGEATQSGA RPADRYGLLK HSREFLDFFW DIAKPEQETR LAATEKLLEY 70 80 90 100 110 120 LRGRPKGSEM KYALKRLITG LGVGRETARP CYSLALAQLL QSFEDLPLCS ILQQIQEKYD 130 140 150 160 170 180 LHQVKKAMLR PALFANLFGV LALFQSGRLV KDQEALMKSV KLLQALAQYQ NHLQEQPRKA 190 200 210 220 230 240 LVDILSEVSK ATLQEILPEV LKADLNIILS SPEQLELFLL AQQKVPSKLK KLVGSVNLFS 250 260 270 280 290 300 DENVPRLVNV LKMAASSVKK DRKLPAIALD LLRLALKEDK FPRFWKEVVE QGLLKMQFWP 310 320 330 340 350 360 ASYLCFRLLG AALPLLTKEQ LHLVMQGDVI RHYGEHVCTA KLPKQFKFAP EMDDYVGTFL 370 380 390 400 410 420 EGCQDDPERQ LAVLVAFSSV TNQGLPVTPT FWRVVRFLSP PALQGYVAWL RAMFLQPDLD 430 440 450 460 470 480 SLVDFSTNNQ KKAQDSSLHM PERAVFRLRK WIIFRLVSIV DSLHLEMEEA LTEQVARFCL 490 500 510 520 530 540 FHSFFVTKKP TSQIPETKHP FSFPLENQAR EAVSSAFFSL LQTLSTQFKQ APGQTQGGQP 550 560 570 580 590 600 WTYHLVQFAD LLLNHSHNVT TVTPFTAQQR QAWDRMLQTL KELEAHSAEA RAAAFQHLLL 610 620 630 640 650 660 LVGIHLLKSP AESCDLLGDI QTCIRKSLGE KPRRSRTKTI DPQEPPWVEV LVEILLALLA 670 680 690 700 710 720 QPSHLMRQVA RSVFGHICSH LTPRALQLIL DVLNPETSED ENDRVVVTDD SDERRLKGAE 730 740 750 760 770 780 DKSEEGEDNR SSESEEESEG EESEEEERDG DVDQGFREQL MTVLQAGKAL GGEDSENEEE 790 800 810 820 830 840 LGDEAMMALD QSLASLFAEQ KLRIQARRDE KNKLQKEKAL RRDFQIRVLD LVEVLVTKQP 850 860 870 880 890 900 ENALVLELLE PLLSIIRRSL RSSSSKQEQD LLHKTARIFT HHLCRARRYC HDLGERAGAL 910 920 930 940 950 960 HAQVERLVQQ AGRQPDSPTA LYHFNASLYL LRVLKGNTAE GCVHETQEKQ KAGTDPSHMP 970 980 990 1000 1010 1020 TGPQAASCLD LNLVTRVYST ALSSFLTKRN SPLTVPMFLS LFSRHPVLCQ SLLPILVQHI 1030 1040 1050 1060 1070 1080 TGPVRPRHQA CLLLQKTLSM REVRSCFEDP EWKQLMGQVL AKVTENLRVL GEAQTKAQHQ 1090 1100 1110 1120 1130 1140 QALSSLELLN VLFRTCKHEK LTLDLTVLLG VLQGQQQSLQ QGAHSTGSSR LHDLYWQAMK 1150 1160 1170 1180 1190 1200 TLGVQRPKLE KKDAKEIPSA TQSPISKKRK KKGFLPETKK RKKRKSEDGT PAEDGTPAAT 1210 1220 1230 1240 1250 1260 GGSQPPSMGR KKRNRTKAKV PAQANGTPTT KSPAPGAPTR SPSTPAKSPK LQKKNQKPSQ 1270 1280 1290 1300 1310 1320 VNGAPGSPTE PAGQKQHQKA LPKKGVLGKS PLSALARKKA RLSLVIRSPS LLQSGAKKKA 1330 QTLRFTISSS KK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-1328 (ISOFORM 2). Tissue: Amygdala.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 875-1328 (ISOFORM 1). Tissue: Testis.
[5]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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, MASS SPECTROMETRY.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00005024. IPI00607584.
PIR	T42680.
RefSeq	NP_001099008.1. NM_001105538.1. NP_055335.2. NM_014520.3.
UniGene	Hs.701718.
3D structure databases
ProteinModelPortal	Q9BQG0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BQG0. 17 interactions.
MINT	MINT-1150245.
STRING	9606.ENSP00000370968.
PTM databases
PhosphoSite	Q9BQG0.
Polymorphism databases
DMDM	71153825.
2D gel databases
SWISS-2DPAGE	Q9BQG0.
Proteomic databases
PaxDb	Q9BQG0.
PRIDE	Q9BQG0.
Protocols and materials databases
DNASU	10514.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000254718; ENSP00000254718; ENSG00000132382. ENST00000381556; ENSP00000370968; ENSG00000132382.
GeneID	10514.
KEGG	hsa:10514.
UCSC	uc002fxz.4. human. uc002fyb.4. human.
Organism-specific databases
CTD	10514.
GeneCards	GC17M004442.
H-InvDB	HIX0013445.
HGNC	HGNC:7546. MYBBP1A.
HPA	HPA005466.
MIM	604885. gene.
neXtProt	NX_Q9BQG0.
PharmGKB	PA31346.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG313877.
HOGENOM	HOG000113488.
HOVERGEN	HBG081961.
KO	K02331.
OMA	HKTARIF.
OrthoDB	EOG4RFKRW.
PhylomeDB	Q9BQG0.
Gene expression databases
Bgee	Q9BQG0.
CleanEx	HS_MYBBP1A.
Genevestigator	Q9BQG0.
GermOnline	ENSG00000132382. Homo sapiens.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR007015. DNA_pol_V. [Graphical view]
PANTHER	PTHR13213. PTHR13213. 1 hit.
Pfam	PF04931. DNA_pol_phi. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	10514.
NextBio	39876.
PMAP-CutDB	Q9BQG0.
SOURCE	Search...

Entry information

Entry name

MBB1A_HUMAN

Accession

Primary (citable) accession number: Q9BQG0
Secondary accession number(s): Q86VM3 , Q9BW49, Q9P0V5, Q9UF99

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	April 3, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.