Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Receptor protein serine/threonine kinase

Gene

ChALK5

Organism
Gallus gallus (Chicken)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.SAAS annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. receptor signaling protein activity Source: AgBase
  3. receptor signaling protein serine/threonine kinase activity Source: InterPro
  4. transforming growth factor beta binding Source: AgBase
  5. transforming growth factor beta receptor activity, type I Source: AgBase

GO - Biological processi

  1. activation of MAPKK activity Source: Ensembl
  2. angiogenesis Source: Ensembl
  3. anterior/posterior pattern specification Source: Ensembl
  4. artery morphogenesis Source: Ensembl
  5. cardiac epithelial to mesenchymal transition Source: AgBase
  6. collagen fibril organization Source: Ensembl
  7. embryonic cranial skeleton morphogenesis Source: Ensembl
  8. endothelial cell activation Source: AgBase
  9. endothelial cell migration Source: Ensembl
  10. germ cell migration Source: Ensembl
  11. heart development Source: AgBase
  12. intracellular signal transduction Source: GOC
  13. kidney development Source: Ensembl
  14. lens development in camera-type eye Source: Ensembl
  15. male gonad development Source: Ensembl
  16. mesenchymal cell differentiation Source: AgBase
  17. negative regulation of chondrocyte differentiation Source: Ensembl
  18. negative regulation of endothelial cell proliferation Source: Ensembl
  19. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  20. neuron fate commitment Source: Ensembl
  21. palate development Source: Ensembl
  22. parathyroid gland development Source: Ensembl
  23. pathway-restricted SMAD protein phosphorylation Source: Ensembl
  24. peptidyl-serine phosphorylation Source: Ensembl
  25. peptidyl-threonine phosphorylation Source: Ensembl
  26. pharyngeal system development Source: Ensembl
  27. positive regulation of apoptotic signaling pathway Source: Ensembl
  28. positive regulation of cell growth Source: Ensembl
  29. positive regulation of cellular component movement Source: Ensembl
  30. positive regulation of endothelial cell proliferation Source: AgBase
  31. positive regulation of filopodium assembly Source: Ensembl
  32. positive regulation of gene expression Source: AgBase
  33. positive regulation of pathway-restricted SMAD protein phosphorylation Source: Ensembl
  34. positive regulation of protein kinase B signaling Source: Ensembl
  35. positive regulation of SMAD protein import into nucleus Source: Ensembl
  36. positive regulation of transcription, DNA-templated Source: AgBase
  37. post-embryonic development Source: Ensembl
  38. regulation of epithelial to mesenchymal transition Source: AgBase
  39. regulation of gene expression Source: AgBase
  40. regulation of protein binding Source: Ensembl
  41. regulation of protein ubiquitination Source: Ensembl
  42. response to cholesterol Source: Ensembl
  43. thymus development Source: Ensembl
  44. transforming growth factor beta receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, ReceptorSAAS annotationImported, Serine/threonine-protein kinaseUniRule annotationSAAS annotation, Transferase

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_195006. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_195008. TGF-beta receptor signaling activates SMADs.
REACT_198125. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_211903. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_214793. Downregulation of TGF-beta receptor signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor protein serine/threonine kinaseSAAS annotation (EC:2.7.11.30SAAS annotation)
Gene namesi
Name:ChALK5Imported
Synonyms:TGFBR1Imported
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 2

Subcellular locationi

GO - Cellular componenti

  1. cell Source: AgBase
  2. endosome Source: Ensembl
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: AgBase
  5. plasma membrane Source: Ensembl
  6. receptor complex Source: Ensembl
  7. tight junction Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000020569.

Family & Domainsi

Sequence similaritiesi

Belongs to the protein kinase superfamily.UniRule annotation
Contains protein kinase domain.SAAS annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000230587.
HOVERGENiHBG054502.
KOiK04674.
OMAiRDMIELT.
OrthoDBiEOG7Q8CN3.
TreeFamiTF314724.

Family and domain databases

InterProiIPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTiSM00467. GS. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06900-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRGTRRLR ALLRLLVAAV LLPRAAALQC YCHLCTKDNF TCVTDGLCFT
60 70 80 90 100
SVTRTADRVI RNSMCIAEID LIPRDRPFIC APSFRDGVTT LPHCCDRDHC
110 120 130 140 150
NKIELPIPTP GPTPGRPASS LGPVELAAVI AGPVCFVCIS LMLILYLCHN
160 170 180 190 200
RTVIHHRVPS EEDPSLDRPF ISEGTTLKDL IYDMTTSGSG SGLPLLVQRT
210 220 230 240 250
IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER SWFREAEIYQ
260 270 280 290 300
TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE
310 320 330 340 350
GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA
360 370 380 390 400
DLGLAVRHDS ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD
410 420 430 440 450
IYAMGLVFWE IARRCSIGGI HEDYQLPYYD LVPSDPSVEE MKKVVCEQKL
460 470 480 490 500
RPNIPNRWQS CEALRVMAKI MRECWYANGA ARLTALRIKK TLSQLSQQEG

IKM
Length:503
Mass (Da):56,509
Last modified:October 1, 2000 - v2
Checksum:i87E16F45C5B0F837
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AADN03002802 Genomic DNA. No translation available.
D14460 mRNA. Translation: BAA03357.2.
PIRiA56693.
RefSeqiNP_989577.1. NM_204246.1.
UniGeneiGga.143.

Genome annotation databases

EnsembliENSGALT00000020598; ENSGALP00000020569; ENSGALG00000012617.
GeneIDi374094.
KEGGigga:374094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AADN03002802 Genomic DNA. No translation available.
D14460 mRNA. Translation: BAA03357.2.
PIRiA56693.
RefSeqiNP_989577.1. NM_204246.1.
UniGeneiGga.143.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000020569.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000020598; ENSGALP00000020569; ENSGALG00000012617.
GeneIDi374094.
KEGGigga:374094.

Organism-specific databases

CTDi7046.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000230587.
HOVERGENiHBG054502.
KOiK04674.
OMAiRDMIELT.
OrthoDBiEOG7Q8CN3.
TreeFamiTF314724.

Enzyme and pathway databases

ReactomeiREACT_195006. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_195008. TGF-beta receptor signaling activates SMADs.
REACT_198125. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_211903. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_214793. Downregulation of TGF-beta receptor signaling.

Miscellaneous databases

NextBioi20813613.
PROiQ06900.

Family and domain databases

InterProiIPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTiSM00467. GS. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a cDNA encoding the chicken receptor protein kinase of the TGF-beta receptor family."
    Nohno T., Sumitomo S., Ishikawa T., Ando C., Nishida S., Noji S., Saito T.
    DNA Seq. 3:393-396(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Activin receptor-like kinase 2 can mediate atrioventricular cushion transformation."
    Lai Y.T., Beason K.B., Brames G.P., Desgrosellier J.S., Cleggett M.C., Shaw M.V., Brown C.B., Barnett J.V.
    Dev. Biol. 222:1-11(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
    International Chicken Genome Sequencing Consortium
    Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
    , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
    Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Red jungle fowlImported.
  4. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Red jungle fowlImported.

Entry informationi

Entry nameiQ06900_CHICK
AccessioniPrimary (citable) accession number: Q06900
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: October 1, 2000
Last modified: March 4, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.