Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13705

- AVR2B_HUMAN

UniProt

Q13705 - AVR2B_HUMAN

Protein

Activin receptor type-2B

Gene

ACVR2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (16 May 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor.1 Publication

    Catalytic activityi

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

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei217 – 2171ATPPROSITE-ProRule annotation
    Active sitei321 – 3211Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi196 – 2049ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. growth factor binding Source: HGNC
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. protein serine/threonine/tyrosine kinase activity Source: Ensembl
    6. protein serine/threonine kinase activity Source: HGNC
    7. receptor signaling protein serine/threonine kinase activity Source: InterPro
    8. transforming growth factor beta-activated receptor activity Source: InterPro

    GO - Biological processi

    1. activation of protein kinase activity Source: Ensembl
    2. activin receptor signaling pathway Source: GOC
    3. anterior/posterior pattern specification Source: HGNC
    4. artery development Source: BHF-UCL
    5. blood vessel remodeling Source: BHF-UCL
    6. BMP signaling pathway Source: BHF-UCL
    7. determination of left/right symmetry Source: Ensembl
    8. embryonic foregut morphogenesis Source: Ensembl
    9. gastrulation with mouth forming second Source: Ensembl
    10. heart development Source: Ensembl
    11. insulin secretion Source: Ensembl
    12. kidney development Source: Ensembl
    13. lung development Source: Ensembl
    14. lymphangiogenesis Source: BHF-UCL
    15. lymphatic endothelial cell differentiation Source: BHF-UCL
    16. mesoderm development Source: Ensembl
    17. odontogenesis of dentin-containing tooth Source: Ensembl
    18. organ growth Source: Ensembl
    19. palate development Source: Ensembl
    20. pancreas development Source: Ensembl
    21. positive regulation of activin receptor signaling pathway Source: HGNC
    22. positive regulation of bone mineralization Source: BHF-UCL
    23. positive regulation of osteoblast differentiation Source: BHF-UCL
    24. post-embryonic development Source: Ensembl
    25. regulation of transcription, DNA-templated Source: HGNC
    26. response to glucose Source: Ensembl
    27. retina vasculature development in camera-type eye Source: BHF-UCL
    28. signal transduction Source: HGNC
    29. skeletal system morphogenesis Source: Ensembl
    30. transmembrane receptor protein serine/threonine kinase signaling pathway Source: ProtInc
    31. venous blood vessel development Source: BHF-UCL

    Keywords - Molecular functioni

    Kinase, Receptor, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_111057. Signaling by NODAL.
    REACT_111059. Regulation of signaling by NODAL.
    REACT_12034. Signaling by BMP.
    REACT_150238. Signaling by Activin.
    SignaLinkiQ13705.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Activin receptor type-2B (EC:2.7.11.30)
    Alternative name(s):
    Activin receptor type IIB
    Short name:
    ACTR-IIB
    Gene namesi
    Name:ACVR2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:174. ACVR2B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: Reactome
    4. protein complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Heterotaxy, visceral, 4, autosomal (HTX4) [MIM:613751]: A form of visceral heterotaxy, a complex disorder due to disruption of the normal left-right asymmetry of the thoracoabdominal organs. Visceral heterotaxy or situs ambiguus results in randomization of the placement of visceral organs, including the heart, lungs, liver, spleen, and stomach. The organs are oriented randomly with respect to the left-right axis and with respect to one another. It can been associated with variety of congenital defects including cardiac malformations. HTX4 clinical features include dextrocardia, right aortic arch and a right-sided spleen, anomalies of the inferior and the superior vena cava, atrial ventricular canal defect with dextro-transposed great arteries, pulmonary stenosis, polysplenia and midline liver.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401R → H in HTX4. 1 Publication
    Corresponds to variant rs121434437 [ dbSNP | Ensembl ].
    VAR_013281
    Natural varianti494 – 4941V → I in HTX4. 1 Publication
    VAR_013282

    Keywords - Diseasei

    Disease mutation, Heterotaxy

    Organism-specific databases

    MIMi613751. phenotype.
    Orphaneti157769. Situs ambiguus.
    PharmGKBiPA24495.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 512494Activin receptor type-2BPRO_0000024404Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 591 Publication
    Glycosylationi42 – 421N-linked (GlcNAc...)1 Publication
    Disulfide bondi49 ↔ 771 Publication
    Glycosylationi65 – 651N-linked (GlcNAc...)1 Publication
    Disulfide bondi84 ↔ 1031 Publication
    Disulfide bondi90 ↔ 1021 Publication
    Disulfide bondi104 ↔ 1091 Publication

    Post-translational modificationi

    Phosphorylated. Constitutive phosphorylation is in part catalyzed by its own kinase activity.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ13705.
    PRIDEiQ13705.

    PTM databases

    PhosphoSiteiQ13705.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13705.
    BgeeiQ13705.
    CleanExiHS_ACVR2B.
    GenevestigatoriQ13705.

    Organism-specific databases

    HPAiCAB025115.

    Interactioni

    Subunit structurei

    Forms an activin receptor complex with activin type II receptors such as ACVR1B. Interacts with VPS39.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MSTNO147934EBI-1383577,EBI-8542977

    Protein-protein interaction databases

    BioGridi106608. 22 interactions.
    IntActiQ13705. 6 interactions.
    MINTiMINT-3028545.
    STRINGi9606.ENSP00000340361.

    Structurei

    Secondary structure

    1
    512
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 337
    Helixi36 – 394
    Beta strandi43 – 497
    Beta strandi57 – 6610
    Beta strandi69 – 7911
    Helixi82 – 843
    Beta strandi88 – 914
    Beta strandi98 – 1069
    Turni107 – 1104
    Beta strandi111 – 1144
    Beta strandi191 – 1977
    Beta strandi200 – 20910
    Beta strandi212 – 2198
    Helixi221 – 2233
    Helixi224 – 23512
    Beta strandi247 – 2537
    Turni256 – 2583
    Beta strandi260 – 2667
    Helixi273 – 2797
    Helixi284 – 30219
    Beta strandi305 – 3084
    Turni309 – 3113
    Beta strandi312 – 3143
    Beta strandi316 – 3183
    Helixi324 – 3263
    Beta strandi327 – 3293
    Beta strandi335 – 3373
    Beta strandi344 – 3463
    Helixi362 – 3643
    Helixi367 – 3704
    Helixi378 – 39821
    Turni413 – 4175
    Helixi424 – 4318
    Helixi442 – 4465
    Helixi448 – 46013
    Helixi465 – 4673
    Helixi471 – 48212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H62X-ray1.85D19-116[»]
    2QLUX-ray2.00A190-487[»]
    4FAOX-ray3.36E/F/K/L/Q/R/W/X/e/f/k/l19-134[»]
    ProteinModelPortaliQ13705.
    SMRiQ13705. Positions 24-116, 190-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13705.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 137119ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini159 – 512354CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei138 – 15821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini190 – 480291Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG054502.
    InParanoidiQ13705.
    KOiK13596.
    OMAiKKMRPAI.
    OrthoDBiEOG7JHM5B.
    PhylomeDBiQ13705.
    TreeFamiTF352876.

    Family and domain databases

    InterProiIPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR000333. TGFB_receptor.
    [Graphical view]
    PANTHERiPTHR23255. PTHR23255. 1 hit.
    PfamiPF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR00653. ACTIVIN2R.
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform ActR-IIB2 (identifier: Q13705-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MTAPWVALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE    50
    GEQDKRLHCY ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY 100
    FCCCEGNFCN ERFTHLPEAG GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS 150
    LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP PSPLVGLKPL QLLEIKARGR 200
    FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK HENLLQFIAA 250
    EKRGSNLEVE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY 300
    LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK 350
    PPGDTHGQVG TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC 400
    KAADGPVDEY MLPFEEEIGQ HPSLEELQEV VVHKKMRPTI KDHWLKHPGL 450
    AQLCVTIEEC WDHDAEARLS AGCVEERVSL IRRSVNGTTS DCLVSLVTSV 500
    TNVDLPPKES SI 512
    Length:512
    Mass (Da):57,724
    Last modified:May 16, 2006 - v3
    Checksum:iB377FEF92EF74937
    GO
    Isoform ActR-IIB1 (identifier: Q13705-2)

    Sequence is not available

    Note: Produced from the insertion in the transcript of 82 base pairs, leading to frameshift and protein truncation. May be not functional.

    Length:
    Mass (Da):

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 172CA → WP in CAA54671. (PubMed:8161782)Curated
    Sequence conflicti64 – 641R → A(PubMed:8161782)Curated
    Sequence conflicti64 – 641R → A(PubMed:9621519)Curated
    Sequence conflicti459 – 4591E → A in AAC64515. (PubMed:9916847)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401R → H in HTX4. 1 Publication
    Corresponds to variant rs121434437 [ dbSNP | Ensembl ].
    VAR_013281
    Natural varianti176 – 1761P → R.1 Publication
    Corresponds to variant rs35882617 [ dbSNP | Ensembl ].
    VAR_041396
    Natural varianti459 – 4591E → D.1 Publication
    Corresponds to variant rs500611 [ dbSNP | Ensembl ].
    VAR_050594
    Natural varianti494 – 4941V → I in HTX4. 1 Publication
    VAR_013282

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77533 mRNA. Translation: CAA54671.1.
    AB008681 Genomic DNA. Translation: BAA24180.2.
    AF060202
    , AF060199, AF060200, AF060201 Genomic DNA. Translation: AAC64515.1.
    BC096243 mRNA. Translation: AAH96243.1.
    BC096244 mRNA. Translation: AAH96244.1.
    BC099642 mRNA. Translation: AAH99642.1.
    CCDSiCCDS2679.1. [Q13705-1]
    PIRiI37134.
    RefSeqiNP_001097.2. NM_001106.3. [Q13705-1]
    UniGeneiHs.174273.

    Genome annotation databases

    EnsembliENST00000352511; ENSP00000340361; ENSG00000114739. [Q13705-1]
    GeneIDi93.
    KEGGihsa:93.
    UCSCiuc003cif.3. human. [Q13705-1]

    Polymorphism databases

    DMDMi97535735.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77533 mRNA. Translation: CAA54671.1 .
    AB008681 Genomic DNA. Translation: BAA24180.2 .
    AF060202
    , AF060199 , AF060200 , AF060201 Genomic DNA. Translation: AAC64515.1 .
    BC096243 mRNA. Translation: AAH96243.1 .
    BC096244 mRNA. Translation: AAH96244.1 .
    BC099642 mRNA. Translation: AAH99642.1 .
    CCDSi CCDS2679.1. [Q13705-1 ]
    PIRi I37134.
    RefSeqi NP_001097.2. NM_001106.3. [Q13705-1 ]
    UniGenei Hs.174273.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H62 X-ray 1.85 D 19-116 [» ]
    2QLU X-ray 2.00 A 190-487 [» ]
    4FAO X-ray 3.36 E/F/K/L/Q/R/W/X/e/f/k/l 19-134 [» ]
    ProteinModelPortali Q13705.
    SMRi Q13705. Positions 24-116, 190-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106608. 22 interactions.
    IntActi Q13705. 6 interactions.
    MINTi MINT-3028545.
    STRINGi 9606.ENSP00000340361.

    Chemistry

    BindingDBi Q13705.
    ChEMBLi CHEMBL5466.
    GuidetoPHARMACOLOGYi 1792.

    PTM databases

    PhosphoSitei Q13705.

    Polymorphism databases

    DMDMi 97535735.

    Proteomic databases

    PaxDbi Q13705.
    PRIDEi Q13705.

    Protocols and materials databases

    DNASUi 93.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000352511 ; ENSP00000340361 ; ENSG00000114739 . [Q13705-1 ]
    GeneIDi 93.
    KEGGi hsa:93.
    UCSCi uc003cif.3. human. [Q13705-1 ]

    Organism-specific databases

    CTDi 93.
    GeneCardsi GC03P038470.
    HGNCi HGNC:174. ACVR2B.
    HPAi CAB025115.
    MIMi 602730. gene.
    613751. phenotype.
    neXtProti NX_Q13705.
    Orphaneti 157769. Situs ambiguus.
    PharmGKBi PA24495.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG054502.
    InParanoidi Q13705.
    KOi K13596.
    OMAi KKMRPAI.
    OrthoDBi EOG7JHM5B.
    PhylomeDBi Q13705.
    TreeFami TF352876.

    Enzyme and pathway databases

    Reactomei REACT_111057. Signaling by NODAL.
    REACT_111059. Regulation of signaling by NODAL.
    REACT_12034. Signaling by BMP.
    REACT_150238. Signaling by Activin.
    SignaLinki Q13705.

    Miscellaneous databases

    EvolutionaryTracei Q13705.
    GeneWikii ACVR2B.
    GenomeRNAii 93.
    NextBioi 351.
    PROi Q13705.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13705.
    Bgeei Q13705.
    CleanExi HS_ACVR2B.
    Genevestigatori Q13705.

    Family and domain databases

    InterProi IPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR000333. TGFB_receptor.
    [Graphical view ]
    PANTHERi PTHR23255. PTHR23255. 1 hit.
    Pfami PF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR00653. ACTIVIN2R.
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of type II activin receptor genes during differentiation of human K562 cells and cDNA cloning of the human type IIB activin receptor."
      Hilden K., Tuuri T., Eramaa M., Ritvos O.
      Blood 83:2163-2170(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Genomic organization and mapping of the human activin receptor type IIB (hActR-IIB) gene."
      Ishikawa S., Kai M., Murata Y., Tamari M., Daigo Y., Murano T., Ogawa M., Nakamura Y.
      J. Hum. Genet. 43:132-134(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASP-459.
    3. "Left-right axis malformations associated with mutations in ACVR2B, the gene for human activin receptor type IIB."
      Kosaki R., Gebbia M., Kosaki K., Lewin M., Bowers P., Towbin J.A., Casey B.
      Am. J. Med. Genet. 82:70-76(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANTS HTX4 HIS-40 AND ILE-494.
    4. "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].
    5. "Activation of signalling by the activin receptor complex."
      Attisano L., Wrana J.L., Montalvo E., Massague J.
      Mol. Cell. Biol. 16:1066-1073(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH ACVR1B, FUNCTION IN PHOSPHORYLATION OF ACVR1B.
    6. "TLP, a novel modulator of TGF-beta signaling, has opposite effects on Smad2- and Smad3-dependent signaling."
      Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S., McNally J.G., Roberts A.B.
      EMBO J. 22:4465-4477(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VPS39.
    7. "Specificity and structure of a high affinity activin receptor-like kinase 1 (ALK1) signaling complex."
      Townson S.A., Martinez-Hackert E., Greppi C., Lowden P., Sako D., Liu J., Ucran J.A., Liharska K., Underwood K.W., Seehra J., Kumar R., Grinberg A.V.
      J. Biol. Chem. 287:27313-27325(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.36 ANGSTROMS) OF 19-134 IN COMPLEX WITH ACVRL1 AND BMP9, DISULFIDE BONDS, GLYCOSYLATION AT ASN-42 AND ASN-65.
    8. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-176.

    Entry informationi

    Entry nameiAVR2B_HUMAN
    AccessioniPrimary (citable) accession number: Q13705
    Secondary accession number(s): Q4VAV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 157 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3