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O35821

- MBB1A_RAT

UniProt

O35821 - MBB1A_RAT

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Protein

Myb-binding protein 1A

Gene

Mybbp1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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) (By similarity).By similarity

GO - Molecular functioni

  1. DNA-directed DNA polymerase activity Source: InterPro
  2. poly(A) RNA binding Source: Ensembl
  3. sequence-specific DNA binding Source: RGD

GO - Biological processi

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

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Myb-binding protein 1A
Alternative name(s):
PAR-interacting protein
Short name:
PIP
Gene namesi
Name:Mybbp1a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi62062. Mybbp1a.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. membrane Source: Ensembl
  3. NLS-dependent protein nuclear import complex Source: UniProtKB
  4. nucleolus Source: UniProtKB
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 13441343Myb-binding protein 1APRO_0000096257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei69 – 691N6-acetyllysineBy similarity
Modified residuei156 – 1561N6-acetyllysineBy similarity
Modified residuei1162 – 11621PhosphoserineBy similarity
Modified residuei1166 – 11661PhosphoserineBy similarity
Modified residuei1189 – 11891PhosphoserineBy similarity
Modified residuei1193 – 11931PhosphothreonineBy similarity
Modified residuei1221 – 12211PhosphoserineBy similarity
Modified residuei1246 – 12461PhosphoserineBy similarity
Modified residuei1255 – 12551PhosphoserineBy similarity
Modified residuei1280 – 12801PhosphothreonineBy similarity
Modified residuei1283 – 12831PhosphoserineBy similarity
Modified residuei1305 – 13051PhosphoserineBy similarity
Modified residuei1318 – 13181PhosphoserineBy similarity
Modified residuei1322 – 13221CitrullineBy similarity
Modified residuei1323 – 13231PhosphoserineBy similarity
Modified residuei1325 – 13251PhosphoserineBy similarity
Modified residuei1329 – 13291PhosphoserineBy similarity

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

PaxDbiO35821.
PRIDEiO35821.

PTM databases

PhosphoSiteiO35821.

Expressioni

Gene expression databases

GenevestigatoriO35821.

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

Protein-protein interaction databases

IntActiO35821. 1 interaction.
STRINGi10116.ENSRNOP00000021134.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 580579Interaction with MYBBy similarityAdd
BLAST
Regioni1154 – 1344191Required for nuclear and nucleolar localizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi238 – 25619Nuclear export signal 1By similarityAdd
BLAST
Motifi261 – 27919Nuclear export signal 2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi694 – 78188Glu-richAdd
BLAST

Phylogenomic databases

eggNOGiNOG313877.
GeneTreeiENSGT00390000017457.
HOGENOMiHOG000113488.
HOVERGENiHBG081961.
InParanoidiO35821.
KOiK02331.
OMAiHQAQACL.
OrthoDBiEOG7G7KPN.
PhylomeDBiO35821.
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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35821 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEMKSPTKA EPASPAEAPQ GDRRSLLEHS REFLDFFWDI AKPDQETRLR
60 70 80 90 100
ATEKLLEYLR TRPSDSEMKY ALKRLITGLG VGREAARPCY SLALAQLLQS
110 120 130 140 150
FEDIQLCDIL GQIQEKYNLQ AMNKAMMRPT LFANLFGVLA LFQSGRLVKD
160 170 180 190 200
KEALMKCVRL LKILSHHYNH LQGQPVKALV DILSEVPESM FQEILPKVLK
210 220 230 240 250
GDMKVILSSP KYLELFLLAR QRVPAELESL VGSVDLFSED NIPSLVNILK
260 270 280 290 300
VAANSVKKEQ KLPDVALNLL RLALQENKFE RFWKEVLEEG LLKKPSYTSS
310 320 330 340 350
YMCFRLLGAS LPLLSDEQLQ LVMRGDLIRH FGEHMVVSKS QNPLRFIPEI
360 370 380 390 400
SAYVGTFLEG CQDDPKRQFT VMVAFTAITN QGLPVMPTFW RVTRFLNTEA
410 420 430 440 450
LQNYVTWLRD MFLQPDLDSL VDFSTANQKR VQVASLNVPE RTVFRLRKWI
460 470 480 490 500
IHRLVSLVDH LHLEKDEAVV EQIARFCLFH AFFKTKKATP QIPETKQHFS
510 520 530 540 550
FPLEDGNRGV IVSAFFSLLQ TLSVKFRQTP DLAENGKPWT YRLVQLADML
560 570 580 590 600
LKHNRNVANV TPLTAQQRQA WDQMMSTLKE LEAQSSETRA IAFQHLLLLV
610 620 630 640 650
GLHLFKSPAE SCDVLGDIQT CIKKSMEQNL RRSRSRAKAS QEPVWVEVMV
660 670 680 690 700
EILLSLLAQP SNLMRQVVRS VFGHVCSHLT PRGLQLILAV LNPETNEDEE
710 720 730 740 750
DNVVVTDTDE KQLKHGEDAD SDSEDSKNSE SDVDSEDGEE SEEEDRDKDV
760 770 780 790 800
DPGFRQQLME VLQAGNALGG EEEEEEELGD EAMMALDQNL ASLFAEQKMR
810 820 830 840 850
IQARHEEKNK LQKEKQLRRD FQIRALDLIE VLVTKQPEHP LILELLEPLL
860 870 880 890 900
NIIQRSMRSR GSTKQEQDLL HKTARIFMHH LCRARHYCHE VEPGAEALHA
910 920 930 940 950
QVERLVQQAG NQADASVALY YFNASLYLLR VLKGNTTKRY QDGQKLEGAD
960 970 980 990 1000
IKSEPKDSEV QTTSCLDLDF VTRVYSASLE SLLTKRNSPL TIPMFLDLFS
1010 1020 1030 1040 1050
RYPVICKNLL PIVVQHVAGS SRPRHQAQAC LLLQKALSAR ELRVCFEDPE
1060 1070 1080 1090 1100
WEQLISQVLG KTTQTLQTLG EAQSKGEHQR ELSILELLNT VFRIVNHEKL
1110 1120 1130 1140 1150
SVDLTAFLGM LQGKQQKLQQ NLQQGNHSSG SSRLYDLYWQ AMNLLGVQRP
1160 1170 1180 1190 1200
KSEKKNVKDI PSDSQSPIST KRKKKGFLPE TKKRKKLKSE GTTSEKKAAS
1210 1220 1230 1240 1250
QQDAVTEGAM PAATGKDQPP STGKKRRKRV KANTPSQVNG VTVAKSPAPN
1260 1270 1280 1290 1300
NPTLSPSTPP AKTPKVQKKK EKLSQVNGST PVSPVEPESK KHQKALSTKE
1310 1320 1330 1340
VKRRSSQSAL PKKRARLSLV SRSPSLLQSG IRKRRVARRR VQTP
Length:1,344
Mass (Da):152,286
Last modified:July 19, 2005 - v2
Checksum:iA5721894AD80BDF0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371G → A in AAB62878. 1 PublicationCurated
Sequence conflicti433 – 4331V → D in AAB62878. 1 PublicationCurated
Sequence conflicti905 – 9051L → F in AAB62878. 1 PublicationCurated
Sequence conflicti1204 – 12041A → R in AAB62878. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03073819 Genomic DNA. No translation available.
U83590 mRNA. Translation: AAB62878.1.
PIRiT32731.
RefSeqiNP_113856.1. NM_031668.1.
XP_006246864.1. XM_006246802.1.
UniGeneiRn.35696.

Genome annotation databases

EnsembliENSRNOT00000021134; ENSRNOP00000021134; ENSRNOG00000015236.
GeneIDi60571.
KEGGirno:60571.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03073819 Genomic DNA. No translation available.
U83590 mRNA. Translation: AAB62878.1 .
PIRi T32731.
RefSeqi NP_113856.1. NM_031668.1.
XP_006246864.1. XM_006246802.1.
UniGenei Rn.35696.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O35821. 1 interaction.
STRINGi 10116.ENSRNOP00000021134.

PTM databases

PhosphoSitei O35821.

Proteomic databases

PaxDbi O35821.
PRIDEi O35821.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021134 ; ENSRNOP00000021134 ; ENSRNOG00000015236 .
GeneIDi 60571.
KEGGi rno:60571.

Organism-specific databases

CTDi 10514.
RGDi 62062. Mybbp1a.

Phylogenomic databases

eggNOGi NOG313877.
GeneTreei ENSGT00390000017457.
HOGENOMi HOG000113488.
HOVERGENi HBG081961.
InParanoidi O35821.
KOi K02331.
OMAi HQAQACL.
OrthoDBi EOG7G7KPN.
PhylomeDBi O35821.
TreeFami TF317401.

Miscellaneous databases

NextBioi 612270.
PROi O35821.

Gene expression databases

Genevestigatori O35821.

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

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Isolation of PIP, a 160 kDa nucleolar protein that interacts with the activation domain of PAR transcription factors."
    Comte P.A., Ossipow V., Schibler U.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-1344.

Entry informationi

Entry nameiMBB1A_RAT
AccessioniPrimary (citable) accession number: O35821
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: October 29, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3