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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.

GO - Molecular functioni

  1. DNA-directed DNA polymerase activity Source: InterPro
  2. 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. positive regulation of cell cycle arrest Source: Ensembl
  6. respiratory electron transport chain Source: Ensembl
  7. 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.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 13441343Myb-binding protein 1A
PRO_0000096257Add
BLAST

Amino acid modifications

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

Protein-protein interaction databases

IntActiO35821. 1 interaction.
STRINGi10116.ENSRNOP00000021134.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 580579Interaction with MYB By similarity
Add
BLAST
Regioni1154 – 1344191Required for nuclear and nucleolar localization By similarity
Add
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi694 – 78188Glu-rich
Add
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.

O35821-1 [UniParc]FASTAAdd to Basket

« Hide

MAEMKSPTKA EPASPAEAPQ GDRRSLLEHS REFLDFFWDI AKPDQETRLR     50
ATEKLLEYLR TRPSDSEMKY ALKRLITGLG VGREAARPCY SLALAQLLQS 100
FEDIQLCDIL GQIQEKYNLQ AMNKAMMRPT LFANLFGVLA LFQSGRLVKD 150
KEALMKCVRL LKILSHHYNH LQGQPVKALV DILSEVPESM FQEILPKVLK 200
GDMKVILSSP KYLELFLLAR QRVPAELESL VGSVDLFSED NIPSLVNILK 250
VAANSVKKEQ KLPDVALNLL RLALQENKFE RFWKEVLEEG LLKKPSYTSS 300
YMCFRLLGAS LPLLSDEQLQ LVMRGDLIRH FGEHMVVSKS QNPLRFIPEI 350
SAYVGTFLEG CQDDPKRQFT VMVAFTAITN QGLPVMPTFW RVTRFLNTEA 400
LQNYVTWLRD MFLQPDLDSL VDFSTANQKR VQVASLNVPE RTVFRLRKWI 450
IHRLVSLVDH LHLEKDEAVV EQIARFCLFH AFFKTKKATP QIPETKQHFS 500
FPLEDGNRGV IVSAFFSLLQ TLSVKFRQTP DLAENGKPWT YRLVQLADML 550
LKHNRNVANV TPLTAQQRQA WDQMMSTLKE LEAQSSETRA IAFQHLLLLV 600
GLHLFKSPAE SCDVLGDIQT CIKKSMEQNL RRSRSRAKAS QEPVWVEVMV 650
EILLSLLAQP SNLMRQVVRS VFGHVCSHLT PRGLQLILAV LNPETNEDEE 700
DNVVVTDTDE KQLKHGEDAD SDSEDSKNSE SDVDSEDGEE SEEEDRDKDV 750
DPGFRQQLME VLQAGNALGG EEEEEEELGD EAMMALDQNL ASLFAEQKMR 800
IQARHEEKNK LQKEKQLRRD FQIRALDLIE VLVTKQPEHP LILELLEPLL 850
NIIQRSMRSR GSTKQEQDLL HKTARIFMHH LCRARHYCHE VEPGAEALHA 900
QVERLVQQAG NQADASVALY YFNASLYLLR VLKGNTTKRY QDGQKLEGAD 950
IKSEPKDSEV QTTSCLDLDF VTRVYSASLE SLLTKRNSPL TIPMFLDLFS 1000
RYPVICKNLL PIVVQHVAGS SRPRHQAQAC LLLQKALSAR ELRVCFEDPE 1050
WEQLISQVLG KTTQTLQTLG EAQSKGEHQR ELSILELLNT VFRIVNHEKL 1100
SVDLTAFLGM LQGKQQKLQQ NLQQGNHSSG SSRLYDLYWQ AMNLLGVQRP 1150
KSEKKNVKDI PSDSQSPIST KRKKKGFLPE TKKRKKLKSE GTTSEKKAAS 1200
QQDAVTEGAM PAATGKDQPP STGKKRRKRV KANTPSQVNG VTVAKSPAPN 1250
NPTLSPSTPP AKTPKVQKKK EKLSQVNGST PVSPVEPESK KHQKALSTKE 1300
VKRRSSQSAL PKKRARLSLV SRSPSLLQSG IRKRRVARRR VQTP 1344
Length:1,344
Mass (Da):152,286
Last modified:July 19, 2005 - v2
Checksum:iA5721894AD80BDF0
GO

Sequence conflict

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

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: April 16, 2014
This is version 95 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

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