AVR2B_HUMAN
ID AVR2B_HUMAN Reviewed; 512 AA.
AC Q13705; Q4VAV0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Activin receptor type-2B;
DE EC=2.7.11.30;
DE AltName: Full=Activin receptor type IIB;
DE Short=ACTR-IIB;
DE Flags: Precursor;
GN Name=ACVR2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8161782;
RA Hilden K., Tuuri T., Eramaa M., Ritvos O.;
RT "Expression of type II activin receptor genes during differentiation of
RT human K562 cells and cDNA cloning of the human type IIB activin receptor.";
RL Blood 83:2163-2170(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-459.
RX PubMed=9621519; DOI=10.1007/s100380050054;
RA Ishikawa S., Kai M., Murata Y., Tamari M., Daigo Y., Murano T., Ogawa M.,
RA Nakamura Y.;
RT "Genomic organization and mapping of the human activin receptor type IIB
RT (hActR-IIB) gene.";
RL J. Hum. Genet. 43:132-134(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANTS HTX4
RP HIS-40 AND ILE-494.
RX PubMed=9916847;
RX DOI=10.1002/(sici)1096-8628(19990101)82:1<70::aid-ajmg14>3.0.co;2-y;
RA Kosaki R., Gebbia M., Kosaki K., Lewin M., Bowers P., Towbin J.A.,
RA Casey B.;
RT "Left-right axis malformations associated with mutations in ACVR2B, the
RT gene for human activin receptor type IIB.";
RL Am. J. Med. Genet. 82:70-76(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION, INTERACTION WITH ACVR1B, AND FUNCTION IN PHOSPHORYLATION
RP OF ACVR1B.
RX PubMed=8622651; DOI=10.1128/mcb.16.3.1066;
RA Attisano L., Wrana J.L., Montalvo E., Massague J.;
RT "Activation of signalling by the activin receptor complex.";
RL Mol. Cell. Biol. 16:1066-1073(1996).
RN [6]
RP INTERACTION WITH VPS39.
RX PubMed=12941698; DOI=10.1093/emboj/cdg428;
RA Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S.,
RA McNally J.G., Roberts A.B.;
RT "TLP, a novel modulator of TGF-beta signaling, has opposite effects on
RT Smad2- and Smad3-dependent signaling.";
RL EMBO J. 22:4465-4477(2003).
RN [7]
RP INTERACTION WITH BMP6.
RX PubMed=18070108; DOI=10.1111/j.1742-4658.2007.06187.x;
RA Saremba S., Nickel J., Seher A., Kotzsch A., Sebald W., Mueller T.D.;
RT "Type I receptor binding of bone morphogenetic protein 6 is dependent on N-
RT glycosylation of the ligand.";
RL FEBS J. 275:172-183(2008).
RN [8]
RP INTERACTION WITH BMP3, AND SUBCELLULAR LOCATION.
RX PubMed=31665064; DOI=10.1186/s13046-019-1435-1;
RA Wen J., Liu X., Qi Y., Niu F., Niu Z., Geng W., Zou Z., Huang R., Wang J.,
RA Zou H.;
RT "BMP3 suppresses colon tumorigenesis via ActRIIB/SMAD2-dependent and
RT TAK1/JNK signaling pathways.";
RL J. Exp. Clin. Cancer Res. 38:428-428(2019).
RN [9] {ECO:0007744|PDB:2H62}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-116, AND INTERACTION WITH
RP BMP2.
RX PubMed=17295905; DOI=10.1186/1472-6807-7-6;
RA Weber D., Kotzsch A., Nickel J., Harth S., Seher A., Mueller U., Sebald W.,
RA Mueller T.D.;
RT "A silent H-bond can be mutationally activated for high-affinity
RT interaction of BMP-2 and activin type IIB receptor.";
RL BMC Struct. Biol. 7:6-6(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.36 ANGSTROMS) OF 19-134 IN COMPLEX WITH ACVRL1 AND
RP BMP9, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-42 AND ASN-65.
RX PubMed=22718755; DOI=10.1074/jbc.m112.377960;
RA Townson S.A., Martinez-Hackert E., Greppi C., Lowden P., Sako D., Liu J.,
RA Ucran J.A., Liharska K., Underwood K.W., Seehra J., Kumar R.,
RA Grinberg A.V.;
RT "Specificity and structure of a high affinity activin receptor-like kinase
RT 1 (ALK1) signaling complex.";
RL J. Biol. Chem. 287:27313-27325(2012).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-176.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Transmembrane serine/threonine kinase activin type-2 receptor
CC forming an activin receptor complex with activin type-1
CC serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces
CC the activin signal from the cell surface to the cytoplasm and is thus
CC regulating many physiological and pathological processes including
CC neuronal differentiation and neuronal survival, hair follicle
CC development and cycling, FSH production by the pituitary gland, wound
CC healing, extracellular matrix production, immunosuppression and
CC carcinogenesis. Activin is also thought to have a paracrine or
CC autocrine role in follicular development in the ovary. Within the
CC receptor complex, the type-2 receptors act as a primary activin
CC receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-
CC A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream
CC transducers of activin signals. Activin binds to type-2 receptor at the
CC plasma membrane and activates its serine-threonine kinase. The
CC activated receptor type-2 then phosphorylates and activates the type-1
CC receptor. Once activated, the type-1 receptor binds and phosphorylates
CC the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal
CC tail. Soon after their association with the activin receptor and
CC subsequent phosphorylation, SMAD2 and SMAD3 are released into the
CC cytoplasm where they interact with the common partner SMAD4. This SMAD
CC complex translocates into the nucleus where it mediates activin-induced
CC transcription. Inhibitory SMAD7, which is recruited to ACVR1B through
CC FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin
CC receptor complex, thereby blocking the activin signal. Activin signal
CC transduction is also antagonized by the binding to the receptor of
CC inhibin-B via the IGSF1 inhibin coreceptor.
CC {ECO:0000269|PubMed:8622651}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Forms an activin receptor complex with activin type II
CC receptors such as ACVR1B. Interacts with VPS39. Interacts with DYNLT1.
CC Interacts with BMP3 (PubMed:31665064). Interacts with BMP2
CC (PubMed:17295905). Interacts with BMP6 (PubMed:18070108).
CC {ECO:0000250|UniProtKB:P27040, ECO:0000269|PubMed:12941698,
CC ECO:0000269|PubMed:17295905, ECO:0000269|PubMed:18070108,
CC ECO:0000269|PubMed:22718755, ECO:0000269|PubMed:31665064,
CC ECO:0000269|PubMed:8622651}.
CC -!- INTERACTION:
CC Q13705; O14793: MSTN; NbExp=4; IntAct=EBI-1383577, EBI-8542977;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31665064};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=ActR-IIB2;
CC IsoId=Q13705-1; Sequence=Displayed;
CC Name=ActR-IIB1;
CC IsoId=Q13705-2; Sequence=Not described;
CC -!- PTM: Phosphorylated. Constitutive phosphorylation is in part catalyzed
CC by its own kinase activity. {ECO:0000269|PubMed:8622651}.
CC -!- DISEASE: Heterotaxy, visceral, 4, autosomal (HTX4) [MIM:613751]: A form
CC of visceral heterotaxy, a complex disorder due to disruption of the
CC normal left-right asymmetry of the thoracoabdominal organs. Visceral
CC heterotaxy or situs ambiguus results in randomization of the placement
CC of visceral organs, including the heart, lungs, liver, spleen, and
CC stomach. The organs are oriented randomly with respect to the left-
CC right axis and with respect to one another. It can be associated with a
CC variety of congenital defects including cardiac malformations. HTX4
CC clinical features include dextrocardia, right aortic arch and a right-
CC sided spleen, anomalies of the inferior and the superior vena cava,
CC atrial ventricular canal defect with dextro-transposed great arteries,
CC pulmonary stenosis, polysplenia and midline liver.
CC {ECO:0000269|PubMed:9916847}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform ActR-IIB1]: Produced from the insertion in the
CC transcript of 82 base pairs, leading to frameshift and protein
CC truncation. May be not functional. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR EMBL; X77533; CAA54671.1; -; mRNA.
DR EMBL; AB008681; BAA24180.2; -; Genomic_DNA.
DR EMBL; AF060202; AAC64515.1; -; Genomic_DNA.
DR EMBL; AF060199; AAC64515.1; JOINED; Genomic_DNA.
DR EMBL; AF060200; AAC64515.1; JOINED; Genomic_DNA.
DR EMBL; AF060201; AAC64515.1; JOINED; Genomic_DNA.
DR EMBL; BC096243; AAH96243.1; -; mRNA.
DR EMBL; BC096244; AAH96244.1; -; mRNA.
DR EMBL; BC099642; AAH99642.1; -; mRNA.
DR CCDS; CCDS2679.1; -. [Q13705-1]
DR PIR; I37134; I37134.
DR RefSeq; NP_001097.2; NM_001106.3. [Q13705-1]
DR PDB; 2H62; X-ray; 1.85 A; D=19-116.
DR PDB; 2QLU; X-ray; 2.00 A; A=190-487.
DR PDB; 4FAO; X-ray; 3.36 A; E/F/K/L/Q/R/W/X/e/f/k/l=19-134.
DR PDB; 5NGV; X-ray; 2.00 A; A=24-117.
DR PDB; 5NHR; X-ray; 3.35 A; C/D=24-117.
DR PDB; 7MRZ; X-ray; 3.00 A; C=19-134.
DR PDB; 7OLY; X-ray; 3.27 A; C=19-134.
DR PDBsum; 2H62; -.
DR PDBsum; 2QLU; -.
DR PDBsum; 4FAO; -.
DR PDBsum; 5NGV; -.
DR PDBsum; 5NHR; -.
DR PDBsum; 7MRZ; -.
DR PDBsum; 7OLY; -.
DR AlphaFoldDB; Q13705; -.
DR SMR; Q13705; -.
DR BioGRID; 106608; 97.
DR IntAct; Q13705; 31.
DR MINT; Q13705; -.
DR STRING; 9606.ENSP00000340361; -.
DR BindingDB; Q13705; -.
DR ChEMBL; CHEMBL5466; -.
DR DrugCentral; Q13705; -.
DR GuidetoPHARMACOLOGY; 1792; -.
DR GlyGen; Q13705; 2 sites.
DR iPTMnet; Q13705; -.
DR PhosphoSitePlus; Q13705; -.
DR BioMuta; ACVR2B; -.
DR DMDM; 97535735; -.
DR EPD; Q13705; -.
DR jPOST; Q13705; -.
DR MassIVE; Q13705; -.
DR PaxDb; Q13705; -.
DR PeptideAtlas; Q13705; -.
DR PRIDE; Q13705; -.
DR ProteomicsDB; 59666; -. [Q13705-1]
DR ABCD; Q13705; 1 sequenced antibody.
DR Antibodypedia; 12076; 457 antibodies from 33 providers.
DR DNASU; 93; -.
DR Ensembl; ENST00000352511.5; ENSP00000340361.3; ENSG00000114739.14. [Q13705-1]
DR GeneID; 93; -.
DR KEGG; hsa:93; -.
DR MANE-Select; ENST00000352511.5; ENSP00000340361.3; NM_001106.4; NP_001097.2.
DR UCSC; uc003cif.4; human. [Q13705-1]
DR CTD; 93; -.
DR DisGeNET; 93; -.
DR GeneCards; ACVR2B; -.
DR HGNC; HGNC:174; ACVR2B.
DR HPA; ENSG00000114739; Low tissue specificity.
DR MalaCards; ACVR2B; -.
DR MIM; 602730; gene.
DR MIM; 613751; phenotype.
DR neXtProt; NX_Q13705; -.
DR OpenTargets; ENSG00000114739; -.
DR Orphanet; 157769; Situs ambiguus.
DR PharmGKB; PA24495; -.
DR VEuPathDB; HostDB:ENSG00000114739; -.
DR eggNOG; KOG3653; Eukaryota.
DR GeneTree; ENSGT00940000156210; -.
DR HOGENOM; CLU_000288_8_4_1; -.
DR InParanoid; Q13705; -.
DR OMA; NWNELCH; -.
DR OrthoDB; 390511at2759; -.
DR PhylomeDB; Q13705; -.
DR TreeFam; TF352876; -.
DR PathwayCommons; Q13705; -.
DR Reactome; R-HSA-1181150; Signaling by NODAL.
DR Reactome; R-HSA-1433617; Regulation of signaling by NODAL.
DR Reactome; R-HSA-1502540; Signaling by Activin.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR SignaLink; Q13705; -.
DR SIGNOR; Q13705; -.
DR BioGRID-ORCS; 93; 16 hits in 1082 CRISPR screens.
DR ChiTaRS; ACVR2B; human.
DR EvolutionaryTrace; Q13705; -.
DR GeneWiki; ACVR2B; -.
DR GenomeRNAi; 93; -.
DR Pharos; Q13705; Tchem.
DR PRO; PR:Q13705; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q13705; protein.
DR Bgee; ENSG00000114739; Expressed in secondary oocyte and 184 other tissues.
DR Genevisible; Q13705; HS.
DR GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; IPI:BHF-UCL.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019838; F:growth factor binding; IPI:HGNC-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:HGNC-UCL.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0032924; P:activin receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:HGNC-UCL.
DR GO; GO:0060840; P:artery development; ISS:BHF-UCL.
DR GO; GO:0001974; P:blood vessel remodeling; ISS:BHF-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0001946; P:lymphangiogenesis; ISS:BHF-UCL.
DR GO; GO:0060836; P:lymphatic endothelial cell differentiation; ISS:BHF-UCL.
DR GO; GO:0007498; P:mesoderm development; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0035265; P:organ growth; IEA:Ensembl.
DR GO; GO:0031016; P:pancreas development; IEA:Ensembl.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:BHF-UCL.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IDA:HGNC-UCL.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; TAS:ProtInc.
DR GO; GO:0060841; P:venous blood vessel development; ISS:BHF-UCL.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00653; ACTIVIN2R.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Disease variant; Disulfide bond; Glycoprotein; Heterotaxy; Kinase;
KW Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..512
FT /note="Activin receptor type-2B"
FT /id="PRO_0000024404"
FT TOPO_DOM 19..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 190..480
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 491..512
FT /note="Interaction with DYNLT1"
FT /evidence="ECO:0000250|UniProtKB:P27040"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 196..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22718755"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22718755"
FT DISULFID 29..59
FT /evidence="ECO:0000269|PubMed:22718755"
FT DISULFID 49..77
FT /evidence="ECO:0000269|PubMed:22718755"
FT DISULFID 84..103
FT /evidence="ECO:0000269|PubMed:22718755"
FT DISULFID 90..102
FT /evidence="ECO:0000269|PubMed:22718755"
FT DISULFID 104..109
FT /evidence="ECO:0000269|PubMed:22718755"
FT VARIANT 40
FT /note="R -> H (in HTX4; dbSNP:rs121434437)"
FT /evidence="ECO:0000269|PubMed:9916847"
FT /id="VAR_013281"
FT VARIANT 176
FT /note="P -> R (in dbSNP:rs35882617)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041396"
FT VARIANT 459
FT /note="E -> D (in dbSNP:rs500611)"
FT /evidence="ECO:0000269|PubMed:9621519"
FT /id="VAR_050594"
FT VARIANT 494
FT /note="V -> I (in HTX4; dbSNP:rs121434438)"
FT /evidence="ECO:0000269|PubMed:9916847"
FT /id="VAR_013282"
FT CONFLICT 16..17
FT /note="CA -> WP (in Ref. 1; CAA54671)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="R -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="E -> A (in Ref. 3; AAC64515)"
FT /evidence="ECO:0000305"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:2H62"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2H62"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:2H62"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5NGV"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:2H62"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:2H62"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2H62"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2H62"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5NGV"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:2H62"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:2H62"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2H62"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:2QLU"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:2QLU"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:2QLU"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:2QLU"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:2QLU"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 284..302
FT /evidence="ECO:0007829|PDB:2QLU"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:2QLU"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:2QLU"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2QLU"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:2QLU"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2QLU"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:2QLU"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 378..398
FT /evidence="ECO:0007829|PDB:2QLU"
FT TURN 413..417
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 424..431
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 442..446
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 448..460
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:2QLU"
FT HELIX 471..482
FT /evidence="ECO:0007829|PDB:2QLU"
SQ SEQUENCE 512 AA; 57724 MW; B377FEF92EF74937 CRC64;
MTAPWVALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY
ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEAG
GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP
PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK
HENLLQFIAA EKRGSNLEVE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY
LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG
TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ
HPSLEELQEV VVHKKMRPTI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL
IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI
