Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8R149 (BUD13_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BUD13 homolog
Gene names
Name:Bud13
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the CWC26 family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
None. [Check GOA]

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8R149-1)

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: Q8R149-2)

The sequence of this isoform differs from the canonical sequence as follows:
     608-637: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 637637BUD13 homolog
PRO_0000287689

Regions

Coiled coil490 – 53849 Potential
Compositional bias123 – 228106Pro-rich

Amino acid modifications

Modified residue1571Phosphothreonine Ref.4
Modified residue1701Phosphothreonine Ref.4
Modified residue1741Phosphoserine Ref.4
Modified residue2091Phosphothreonine Ref.4
Modified residue2131Phosphoserine Ref.4
Modified residue2221Phosphothreonine Ref.4
Modified residue2261Phosphoserine Ref.4
Modified residue2381Phosphoserine By similarity
Modified residue2591Phosphoserine By similarity
Modified residue2641Phosphoserine By similarity
Modified residue2721Phosphoserine By similarity
Modified residue2971Phosphoserine By similarity
Modified residue3411Phosphoserine Ref.3
Modified residue3441Phosphoserine Ref.3
Modified residue3711Phosphoserine Ref.3
Modified residue3731Phosphoserine Ref.3
Modified residue3761Phosphoserine Ref.3
Modified residue5121Phosphotyrosine By similarity

Natural variations

Alternative sequence608 – 63730Missing in isoform 2.
VSP_025591

Experimental info

Sequence conflict1741S → Y in BAC34509. Ref.1
Sequence conflict1891P → H in BAC34509. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: CA381776034D1A89

FASTA63772,139
        10         20         30         40         50         60 
MAAAPPLTKA EYLKRYLSGT DAGLEGGPEA GRKRRKKRPK PGGAGGKGMR IVDDDVGWAA 

        70         80         90        100        110        120 
ISTAKPEKEE EEDGDLPVVA EFVDERPEEV KQMEAFRSSA KWKLLGGHGE DGHFHHDDQD 

       130        140        150        160        170        180 
SSPPRRVRHD TPDTSPPRKA RHDTPDPSPP RKARHDTPDT SPPRKARHDT PDPSPPRKAR 

       190        200        210        220        230        240 
HDTPDPSPPR RVRHDTPDLS PPRRVRHDTP DLSPPRRVRH DTPDPSPPRR VRHDLDASPP 

       250        260        270        280        290        300 
RKSHRNSSAV SPRRGHHGSL GTSSPRQTHN HSPTAAQHRR TLDSSGTQHL RRAHHESPDL 

       310        320        330        340        350        360 
ELHKAKSSKA AERAPSKAAS QSGLGPSHPS LSTNSKYEHD SDLSPPRKRQ AKAHFEAKKQ 

       370        380        390        400        410        420 
LDSKGVYQKA SDSDLSPPRK KKNSGHQDSD SDLSPPRNRP RRQSSDSDLS PPRRRQRTKS 

       430        440        450        460        470        480 
SDSDLSPPRR SPRPGKKTAH MYSGAKTGLV TDVQREHQEL KKQDQDTTDL GAQFEFTETV 

       490        500        510        520        530        540 
FRDKSGRKRN LKLERLEQRR KAEKDSERDE LYAQWGKGLA QSRQQQQNVE DAMKEMQKPL 

       550        560        570        580        590        600 
ARYIDDEDLD RMLREQEREG DPMANFIKKN KAKENKNKKV KPRYSGPAPP PNRFNIWPGY 

       610        620        630 
RWDGVDRSNG FEQKRFARLA SKKAVEELAY KWSVEDM 

« Hide

Isoform 2 [UniParc].

Checksum: 2DE156A98EABA9AB
Show »

FASTA60768,638

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Thymus and Vagina.
[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).
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-344; SER-371; SER-373 AND SER-376, MASS SPECTROMETRY.
Tissue: Liver.
[4]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157; THR-170; SER-174; THR-209; SER-213; THR-222 AND SER-226, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK037134 mRNA. Translation: BAC29716.1.
AK038126 mRNA. Translation: BAE20531.1.
AK051047 mRNA. Translation: BAC34509.1.
BC025490 mRNA. Translation: AAH25490.1.
IPIIPI00153284.
IPI00845543.
RefSeqNP_666112.1. NM_146000.2.
UniGeneMm.32648.

3D structure databases

ProteinModelPortalQ8R149.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8R149. 11 interactions.
MINTMINT-4118536.

PTM databases

PhosphoSiteQ8R149.

Proteomic databases

PaxDbQ8R149.
PRIDEQ8R149.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000074957; ENSMUSP00000074490; ENSMUSG00000032077.
GeneID215051.
KEGGmmu:215051.
UCSCuc009phi.1. mouse.

Organism-specific databases

CTD84811.
MGIMGI:2443443. Bud13.

Phylogenomic databases

eggNOGNOG317350.
GeneTreeENSGT00390000014500.
HOGENOMHOG000273883.
HOVERGENHBG059757.
InParanoidQ8R149.
KOK13106.
OMASPRRVRH.
OrthoDBEOG40ZQZ9.

Gene expression databases

BgeeQ8R149.
CleanExMM_BUD13.
GenevestigatorQ8R149.

Family and domain databases

InterProIPR018609. Bud13.
[Graphical view]
PfamPF09736. Bud13. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio374592.
SOURCESearch...

Entry information

Entry nameBUD13_MOUSE
AccessionPrimary (citable) accession number: Q8R149
Secondary accession number(s): Q8BQC0, Q8CB03
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2002
Last modified: May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families