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Q9CU19 (Q9CU19_MOUSE) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 92. Feed History...

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

Names and origin

Protein names
Gene names
Name:Acvrl1 MGI 1338946
OrganismMus musculus (Mouse) EMBL BAB31388.2
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length189 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

Ontologies

Keywords
   LigandATP-binding RuleBase RU000304
Nucleotide-binding
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from mutant phenotype PubMed 22783020. Source: MGI

angiogenesis

Inferred from mutant phenotype PubMed 10716993PubMed 11062473. Source: MGI

blood vessel morphogenesis

Inferred from mutant phenotype PubMed 17530030PubMed 17911384. Source: MGI

cellular response to BMP stimulus

Inferred from electronic annotation. Source: Ensembl

endothelial tube morphogenesis

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from mutant phenotype PubMed 17911384. Source: MGI

negative regulation of DNA biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of focal adhesion assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of BMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 14580334. Source: MGI

wound healing, spreading of epidermal cells

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

activin receptor activity, type I

Inferred from electronic annotation. Source: Ensembl

receptor signaling protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor activity, type I

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Experimental info

Non-terminal residue11 EMBL BAB31388.2
Non-terminal residue1891 EMBL BAB31388.2

Sequences

Sequence LengthMass (Da)Tools
Q9CU19 [UniParc].

Last modified March 1, 2003. Version 2.
Checksum: 7A05664B911B7EDF

FASTA18921,067
        10         20         30         40         50         60 
LGRPTEFLNH HCCYRSFCNH NVSLMLEATQ TPSEEPEVDA HLPLILGPVL ALPVLVALGA 

        70         80         90        100        110        120 
LGLWRVRRRQ EKQRDLHSDL GESSLILKAS EQADSMLGDF LDSDCTTGSG SGLPFLVQRT 

       130        140        150        160        170        180 
VARQVALVEC VGKGRYGEVW RGSWHGESVA VKIFSSRDEQ SWFRETEIYN TVLLRHDNIL 


GFIASDMTS 

« Hide

References

[1]"High-efficiency full-length cDNA cloning."
Carninci P., Hayashizaki Y.
Methods Enzymol. 303:19-44(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAB31388.2.
Tissue: Kidney EMBL BAB31388.2.
[2]"Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes."
Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.
Genome Res. 10:1617-1630(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAB31388.2.
Tissue: Kidney EMBL BAB31388.2.
[3]"RIKEN integrated sequence analysis (RISA) system--384-format sequencing pipeline with 384 multicapillary sequencer."
Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A. expand/collapse author list , Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.
Genome Res. 10:1757-1771(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAB31388.2.
Tissue: Kidney EMBL BAB31388.2.
[4]Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H., Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M., Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F. expand/collapse author list , Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H., Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M., Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K., Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T., Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T., Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M., Muramatsu M., Hayashizaki Y.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAB31388.2.
Tissue: Kidney EMBL BAB31388.2.
[5]"Functional annotation of a full-length mouse cDNA collection."
The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium
Nature 409:685-690(2001)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAB31388.2.
Tissue: Kidney EMBL BAB31388.2.
[6]"Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs."
The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team
Nature 420:563-573(2002)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAB31388.2.
Tissue: Kidney EMBL BAB31388.2.
[7]"The Transcriptional Landscape of the Mammalian Genome."
The FANTOM Consortium, Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group)
Science 309:1559-1563(2005)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAB31388.2.
Tissue: Kidney EMBL BAB31388.2.
[8]"Antisense Transcription in the Mammalian Transcriptome."
RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium
Science 309:1564-1566(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAB31388.2.
Tissue: Kidney EMBL BAB31388.2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK018754 mRNA. Translation: BAB31388.2.
UniGeneMm.279542.

3D structure databases

ProteinModelPortalQ9CU19.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000114027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:1338946. Acvrl1.

Phylogenomic databases

HOVERGENHBG054502.
InParanoidQ9CU19.

Gene expression databases

ArrayExpressQ9CU19.
BgeeQ9CU19.
GenevestigatorQ9CU19.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR003605. TGF_beta_rcpt_GS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTSM00467. GS. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameQ9CU19_MOUSE
AccessionPrimary (citable) accession number: Q9CU19
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)