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O35821 (MBB1A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Myb-binding protein 1A
Alternative name(s):
PAR-interacting protein
Short name=PIP
Gene names
Name:Mybbp1a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Subcellular location

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.

Post-translational modification

Citrullinated by PADI4 By similarity.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Molecular functionActivator
Repressor
   PTMAcetylation
Citrullination
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to glucose starvation

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

nucleocytoplasmic transport

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

respiratory electron transport chain

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNLS-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 sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding

Inferred from direct assay PubMed 2261643. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 13441343Myb-binding protein 1A
PRO_0000096257

Regions

Region2 – 580579Interaction with MYB By similarity
Region1154 – 1344191Required for nuclear and nucleolar localization By similarity
Motif238 – 25619Nuclear export signal 1 By similarity
Motif261 – 27919Nuclear export signal 2 By similarity
Compositional bias694 – 78188Glu-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue141Phosphoserine By similarity
Modified residue691N6-acetyllysine By similarity
Modified residue1561N6-acetyllysine By similarity
Modified residue11621Phosphoserine By similarity
Modified residue11661Phosphoserine By similarity
Modified residue11891Phosphoserine By similarity
Modified residue11931Phosphothreonine By similarity
Modified residue12211Phosphoserine By similarity
Modified residue12461Phosphoserine By similarity
Modified residue12551Phosphoserine By similarity
Modified residue12801Phosphothreonine By similarity
Modified residue12831Phosphoserine By similarity
Modified residue13051Phosphoserine By similarity
Modified residue13181Phosphoserine By similarity
Modified residue13221Citrulline By similarity
Modified residue13231Phosphoserine By similarity
Modified residue13251Phosphoserine By similarity
Modified residue13291Phosphoserine By similarity

Experimental info

Sequence conflict1371G → A in AAB62878. Ref.2
Sequence conflict4331V → D in AAB62878. Ref.2
Sequence conflict9051L → F in AAB62878. Ref.2
Sequence conflict12041A → R in AAB62878. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O35821 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: A5721894AD80BDF0

FASTA1,344152,286
        10         20         30         40         50         60 
MAEMKSPTKA EPASPAEAPQ GDRRSLLEHS REFLDFFWDI AKPDQETRLR ATEKLLEYLR 

        70         80         90        100        110        120 
TRPSDSEMKY ALKRLITGLG VGREAARPCY SLALAQLLQS FEDIQLCDIL GQIQEKYNLQ 

       130        140        150        160        170        180 
AMNKAMMRPT LFANLFGVLA LFQSGRLVKD KEALMKCVRL LKILSHHYNH LQGQPVKALV 

       190        200        210        220        230        240 
DILSEVPESM FQEILPKVLK GDMKVILSSP KYLELFLLAR QRVPAELESL VGSVDLFSED 

       250        260        270        280        290        300 
NIPSLVNILK VAANSVKKEQ KLPDVALNLL RLALQENKFE RFWKEVLEEG LLKKPSYTSS 

       310        320        330        340        350        360 
YMCFRLLGAS LPLLSDEQLQ LVMRGDLIRH FGEHMVVSKS QNPLRFIPEI SAYVGTFLEG 

       370        380        390        400        410        420 
CQDDPKRQFT VMVAFTAITN QGLPVMPTFW RVTRFLNTEA LQNYVTWLRD MFLQPDLDSL 

       430        440        450        460        470        480 
VDFSTANQKR VQVASLNVPE RTVFRLRKWI IHRLVSLVDH LHLEKDEAVV EQIARFCLFH 

       490        500        510        520        530        540 
AFFKTKKATP QIPETKQHFS FPLEDGNRGV IVSAFFSLLQ TLSVKFRQTP DLAENGKPWT 

       550        560        570        580        590        600 
YRLVQLADML LKHNRNVANV TPLTAQQRQA WDQMMSTLKE LEAQSSETRA IAFQHLLLLV 

       610        620        630        640        650        660 
GLHLFKSPAE SCDVLGDIQT CIKKSMEQNL RRSRSRAKAS QEPVWVEVMV EILLSLLAQP 

       670        680        690        700        710        720 
SNLMRQVVRS VFGHVCSHLT PRGLQLILAV LNPETNEDEE DNVVVTDTDE KQLKHGEDAD 

       730        740        750        760        770        780 
SDSEDSKNSE SDVDSEDGEE SEEEDRDKDV DPGFRQQLME VLQAGNALGG EEEEEEELGD 

       790        800        810        820        830        840 
EAMMALDQNL ASLFAEQKMR IQARHEEKNK LQKEKQLRRD FQIRALDLIE VLVTKQPEHP 

       850        860        870        880        890        900 
LILELLEPLL NIIQRSMRSR GSTKQEQDLL HKTARIFMHH LCRARHYCHE VEPGAEALHA 

       910        920        930        940        950        960 
QVERLVQQAG NQADASVALY YFNASLYLLR VLKGNTTKRY QDGQKLEGAD IKSEPKDSEV 

       970        980        990       1000       1010       1020 
QTTSCLDLDF VTRVYSASLE SLLTKRNSPL TIPMFLDLFS RYPVICKNLL PIVVQHVAGS 

      1030       1040       1050       1060       1070       1080 
SRPRHQAQAC LLLQKALSAR ELRVCFEDPE WEQLISQVLG KTTQTLQTLG EAQSKGEHQR 

      1090       1100       1110       1120       1130       1140 
ELSILELLNT VFRIVNHEKL SVDLTAFLGM LQGKQQKLQQ NLQQGNHSSG SSRLYDLYWQ 

      1150       1160       1170       1180       1190       1200 
AMNLLGVQRP KSEKKNVKDI PSDSQSPIST KRKKKGFLPE TKKRKKLKSE GTTSEKKAAS 

      1210       1220       1230       1240       1250       1260 
QQDAVTEGAM PAATGKDQPP STGKKRRKRV KANTPSQVNG VTVAKSPAPN NPTLSPSTPP 

      1270       1280       1290       1300       1310       1320 
AKTPKVQKKK EKLSQVNGST PVSPVEPESK KHQKALSTKE VKRRSSQSAL PKKRARLSLV 

      1330       1340 
SRSPSLLQSG IRKRRVARRR VQTP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03073819 Genomic DNA. No translation available.
U83590 mRNA. Translation: AAB62878.1.
PIRT32731.
RefSeqNP_113856.1. NM_031668.1.
XP_006246864.1. XM_006246802.1.
UniGeneRn.35696.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO35821. 1 interaction.
STRING10116.ENSRNOP00000021134.

PTM databases

PhosphoSiteO35821.

Proteomic databases

PaxDbO35821.
PRIDEO35821.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000021134; ENSRNOP00000021134; ENSRNOG00000015236.
GeneID60571.
KEGGrno:60571.

Organism-specific databases

CTD10514.
RGD62062. Mybbp1a.

Phylogenomic databases

eggNOGNOG313877.
GeneTreeENSGT00390000017457.
HOGENOMHOG000113488.
HOVERGENHBG081961.
InParanoidO35821.
KOK02331.
OMAHQAQACL.
OrthoDBEOG7G7KPN.
PhylomeDBO35821.
TreeFamTF317401.

Gene expression databases

GenevestigatorO35821.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR007015. DNA_pol_V.
[Graphical view]
PANTHERPTHR13213. PTHR13213. 1 hit.
PfamPF04931. DNA_pol_phi. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
ProtoNetSearch...

Other

NextBio612270.
PROO35821.

Entry information

Entry nameMBB1A_RAT
AccessionPrimary (citable) accession number: O35821
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program