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P36896 (ACV1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Activin receptor type-1B

EC=2.7.11.30
Alternative name(s):
Activin receptor type IB
Short name=ACTR-IB
Activin receptor-like kinase 4
Short name=ALK-4
Serine/threonine-protein kinase receptor R2
Short name=SKR2
Gene names
Name:ACVR1B
Synonyms:ACVRLK4, ALK4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a 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, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas 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 such as ACVR1B. 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. ACVR1B also phosphorylates TDP2. Ref.2 Ref.9 Ref.10 Ref.13 Ref.16 Ref.19 Ref.20

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Enzyme regulation

Activin receptor type-2 (ACVR2A or ACVR2B) activates the type-1 receptor through phosphorylation of its regulatory GS domain. Ref.11 Ref.14

Subunit structure

Forms an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Interacts with TDP2 By similarity. Interacts with AIP1, FKBP1A, IGSF1, TDGF1, SMAD2, SMAD3 and SMAD7. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.18

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

Expressed in many tissues, most strongly in kidney, pancreas, brain, lung, and liver.

Domain

The GS domain is a 30-amino-acid sequence adjacent to the N-terminal boundary of the kinase domain and highly conserved in all other known type-1 receptors but not in type-2 receptors. The GS domain is the site of activation through phosphorylation by the II receptors. Ref.8

Post-translational modification

Autophosphorylated. Phosphorylated by activin receptor type-2 (ACVR2A or ACVR2B) in response to activin-binding at serine and threonine residues in the GS domain. Phosphorylation of ACVR1B by activin receptor type-2 regulates association with SMAD7. Ref.8 Ref.12 Ref.13 Ref.15 Ref.19

Ubiquitinated. Level of ubiquitination is regulated by the SMAD7-SMURF1 complex. Ref.18 Ref.21

Ubiquitinated.

Involvement in disease

ACVRIB is abundantly expressed in systemic sclerosis patient fibroblasts and production of collagen is also induced by activin-A/INHBA. This suggests that the activin/ACRV1B signaling mechanism is involved in systemic sclerosis.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 GS domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 11117535. Source: HGNC

activin receptor signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

central nervous system development

Inferred from electronic annotation. Source: Ensembl

development of primary female sexual characteristics

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 9884026. Source: BHF-UCL

hair follicle development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from direct assay PubMed 11117535. Source: HGNC

nodal signaling pathway

Inferred from genetic interaction PubMed 11389842. Source: UniProtKB

peptidyl-threonine phosphorylation

Inferred from direct assay Ref.19. Source: UniProtKB

positive regulation of activin receptor signaling pathway

Inferred from direct assay Ref.18. Source: BHF-UCL

positive regulation of erythrocyte differentiation

Inferred from direct assay Ref.9. Source: HGNC

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

positive regulation of trophoblast cell migration

Inferred from direct assay PubMed 21356369. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay Ref.19. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 12065756. Source: HGNC

regulation of transcription, DNA-templated

Inferred from direct assay Ref.17Ref.8. Source: HGNC

signal transduction

Inferred from direct assay Ref.17Ref.8. Source: HGNC

transmembrane receptor protein serine/threonine kinase signaling pathway

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcell surface

Inferred from direct assay Ref.17. Source: HGNC

integral component of plasma membrane

Inferred from direct assay Ref.9. Source: HGNC

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from direct assay PubMed 12065756. Source: HGNC

SMAD binding

Inferred from direct assay PubMed 12065756. Source: HGNC

activin receptor activity, type I

Inferred from direct assay Ref.10. Source: UniProtKB

inhibin binding

Inferred from physical interaction PubMed 7890768. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.11PubMed 11278302PubMed 11389842PubMed 12052855Ref.10. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.19. Source: UniProtKB

receptor signaling protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta-activated receptor activity

Inferred from electronic annotation. Source: InterPro

transmembrane receptor protein serine/threonine kinase activity

Non-traceable author statement Ref.9. Source: HGNC

ubiquitin protein ligase binding

Non-traceable author statement Ref.18. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P36896-1)

Also known as: SKR2-1;

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: P36896-2)

Also known as: SKR2-2;

The sequence of this isoform differs from the canonical sequence as follows:
     465-505: ALRVMGKMMRECWYANGAARLTALRIKKTLSQLSVQEDVKI → VRSWPPAAFPSA
Isoform 3 (identifier: P36896-3)

Also known as: SKR2-3;

The sequence of this isoform differs from the canonical sequence as follows:
     422-505: VHEEYQLPYY...QLSVQEDVKI → TFLFCLCSYL...RLFFRDQFVE
Isoform 4 (identifier: P36896-4)

The sequence of this isoform differs from the canonical sequence as follows:
     271-271: D → ADCSFLTLPWEVVMVSAAPKLRSLRLQYKGGRGRARFLFPLN
Isoform 5 (identifier: P36896-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 505482Activin receptor type-1B
PRO_0000024417

Regions

Topological domain24 – 126103Extracellular Potential
Transmembrane127 – 14923Helical; Potential
Topological domain150 – 505356Cytoplasmic Potential
Domain177 – 20630GS
Domain207 – 497291Protein kinase
Nucleotide binding213 – 2219ATP By similarity

Sites

Active site3351Proton acceptor By similarity
Binding site2341ATP By similarity

Amino acid modifications

Modified residue3801Phosphotyrosine Ref.15
Glycosylation431N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 5252Missing in isoform 5.
VSP_041841
Alternative sequence2711D → ADCSFLTLPWEVVMVSAAPK LRSLRLQYKGGRGRARFLFP LN in isoform 4.
VSP_041842
Alternative sequence422 – 50584VHEEY…EDVKI → TFLFCLCSYLPFQDAGSPKA VLLPPFFLQPVGCLLPEPES SFKVAIKGVEVAVLRVRLFF RDQFVE in isoform 3.
VSP_004953
Alternative sequence465 – 50541ALRVM…EDVKI → VRSWPPAAFPSA in isoform 2.
VSP_004954
Natural variant1461F → L. Ref.23
Corresponds to variant rs34488074 [ dbSNP | Ensembl ].
VAR_041406
Natural variant4081L → V.
Corresponds to variant rs928906 [ dbSNP | Ensembl ].
VAR_011716
Isoform 3:
Natural variant4781R → H.

Experimental info

Mutagenesis401L → A: Increases binding to activin. Ref.17
Mutagenesis701I → A: Decreases binding to activin. Ref.17
Mutagenesis731V → A: Increases binding to activin. Ref.17
Mutagenesis751L → A: Decreases binding to activin. Ref.17
Mutagenesis771P → A: Decreases binding to activin. Ref.17
Mutagenesis2061T → V: Leads to constitutive activation. Ref.8
Sequence conflict561I → F in AAA60555. Ref.3
Sequence conflict561I → F in AAA60556. Ref.3
Sequence conflict222 – 2232WR → MA in AAA60555. Ref.3
Sequence conflict222 – 2232WR → MA in AAA60556. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SKR2-1) [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 40A6C65CAA4C7573

FASTA50556,807
        10         20         30         40         50         60 
MAESAGASSF FPLVVLLLAG SGGSGPRGVQ ALLCACTSCL QANYTCETDG ACMVSIFNLD 

        70         80         90        100        110        120 
GMEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYTDY CNRIDLRVPS GHLKEPEHPS 

       130        140        150        160        170        180 
MWGPVELVGI IAGPVFLLFL IIIIVFLVIN YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ 

       190        200        210        220        230        240 
DLVYDLSTSG SGSGLPLFVQ RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE 

       250        260        270        280        290        300 
ERSWFREAEI YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT 

       310        320        330        340        350        360 
IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA IADLGLAVRH 

       370        380        390        400        410        420 
DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC ADIYALGLVY WEIARRCNSG 

       430        440        450        460        470        480 
GVHEEYQLPY YDLVPSDPSI EEMRKVVCDQ KLRPNIPNWW QSYEALRVMG KMMRECWYAN 

       490        500 
GAARLTALRI KKTLSQLSVQ EDVKI 

« Hide

Isoform 2 (SKR2-2) [UniParc].

Checksum: 13269BD6D04F39D3
Show »

FASTA47653,411
Isoform 3 (SKR2-3) [UniParc].

Checksum: 969525A044E8F7C6
Show »

FASTA48754,270
Isoform 4 [UniParc].

Checksum: 0A75C7D6FE406EB3
Show »

FASTA54661,439
Isoform 5 [UniParc].

Checksum: 8E6885B168A1B026
Show »

FASTA45351,725

References

« Hide 'large scale' references
[1]"Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity."
ten Dijke P., Ichijo H., Franzen P., Schulz P., Saras J., Toyoshima H., Heldin C.-H., Miyazono K.
Oncogene 8:2879-2887(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Type I receptors specify growth-inhibitory and transcriptional responses to transforming growth factor beta and activin."
Carcamo J., Weis F.M., Ventura F., Wieser R., Wrana J.L., Attisano L., Massague J.
Mol. Cell. Biol. 14:3810-3821(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN A ACTIVIN RECEPTOR COMPLEX, ACTIVIN-BINDING, FUNCTION.
Tissue: Kidney.
[3]"Genomic structure and cloned cDNAs predict that four variants in the kinase domain of serine/threonine kinase receptors arise by alternative splicing and poly(A) addition."
Xu J., Matsuzaki K., McKeehan K., Wang F., Kan M., McKeehan W.L.
Proc. Natl. Acad. Sci. U.S.A. 91:7957-7961(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING.
Tissue: Liver.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
[6]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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).
Tissue: Brain and Eye.
[8]"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: INTERACTION WITH ACVR2B, PHOSPHORYLATION BY ACVR2B, DOMAIN GS, MUTAGENESIS OF THR-206.
[9]"Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation."
Lebrun J.J., Vale W.W.
Mol. Cell. Biol. 17:1682-1691(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, FUNCTION.
[10]"Roles of pathway-specific and inhibitory Smads in activin receptor signaling."
Lebrun J.J., Takabe K., Chen Y., Vale W.
Mol. Endocrinol. 13:15-23(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMAD2; SMAD3 AND SMAD7, FUNCTION.
[11]"Modulation of activin signal transduction by inhibin B and inhibin-binding protein (INhBP)."
Chapman S.C., Woodruff T.K.
Mol. Endocrinol. 15:668-679(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGSF1, ENZYME REGULATION.
[12]"Phosphorylation regulation of the interaction between Smad7 and activin type I receptor."
Liu X., Nagarajan R.P., Vale W., Chen Y.
FEBS Lett. 519:93-98(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH SMAD7.
[13]"Overexpression of wild-type activin receptor alk4-1 restores activin antiproliferative effects in human pituitary tumor cells."
Danila D.C., Zhang X., Zhou Y., Haidar J.N., Klibanski A.
J. Clin. Endocrinol. Metab. 87:4741-4746(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[14]"Cripto-1 activates nodal- and ALK4-dependent and -independent signaling pathways in mammary epithelial Cells."
Bianco C., Adkins H.B., Wechselberger C., Seno M., Normanno N., De Luca A., Sun Y., Khan N., Kenney N., Ebert A., Williams K.P., Sanicola M., Salomon D.S.
Mol. Cell. Biol. 22:2586-2597(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TDGF1, ENZYME REGULATION.
[15]"Identification of the phosphotyrosine proteome from thrombin activated platelets."
Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G., Fitzgerald D.J.
Proteomics 2:642-648(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-380.
[16]"Activin signaling through type IB activin receptor stimulates aromatase activity in the ovarian granulosa cell-like human granulosa (KGN) cells."
Mukasa C., Nomura M., Tanaka T., Tanaka K., Nishi Y., Okabe T., Goto K., Yanase T., Nawata H.
Endocrinology 144:1603-1611(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Identification of a functional binding site for activin on the type I receptor ALK4."
Harrison C.A., Gray P.C., Koerber S.C., Fischer W., Vale W.
J. Biol. Chem. 278:21129-21135(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-40; ILE-70; VAL-73; LEU-75 AND PRO-77, ACTIVIN-BINDING.
[18]"FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type I receptor."
Yamaguchi T., Kurisaki A., Yamakawa N., Minakuchi K., Sugino H.
J. Mol. Endocrinol. 36:569-579(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FKBP1A AND SMAD7, UBIQUITINATION.
[19]"Ttrap is an essential modulator of Smad3-dependent Nodal signaling during zebrafish gastrulation and left-right axis determination."
Esguerra C.V., Nelles L., Vermeire L., Ibrahimi A., Crawford A.D., Derua R., Janssens E., Waelkens E., Carmeliet P., Collen D., Huylebroeck D.
Development 134:4381-4393(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOPHOSPHORYLATION.
[20]"Activin A induces neuronal differentiation and survival via ALK4 in a SMAD-independent manner in a subpopulation of human neuroblastomas."
Suzuki K., Kobayashi T., Funatsu O., Morita A., Ikekita M.
Biochem. Biophys. Res. Commun. 394:639-645(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Development and validation of a method for profiling post-translational modification activities using protein microarrays."
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[22]"Activation of the activin A-ALK-Smad pathway in systemic sclerosis."
Takagi K., Kawaguchi Y., Kawamoto M., Ota Y., Tochimoto A., Gono T., Katsumata Y., Takagi M., Hara M., Yamanaka H.
J. Autoimmun. 36:181-188(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SYSTEMIC SCLEROSIS.
[23]"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. expand/collapse author list , 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] LEU-146, VARIANT [LARGE SCALE ANALYSIS] HIS-478 (ISOFORM 3).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z22536 mRNA. Translation: CAA80258.1.
U14722 mRNA. Translation: AAA50246.1.
L10125 mRNA. Translation: AAA60555.1.
L10126 mRNA. Translation: AAA60556.1.
L31848 Genomic DNA. Translation: AAA53349.1.
L31848 Genomic DNA. Translation: AAA53350.1.
L31848 Genomic DNA. Translation: AAA53351.1.
BT007072 mRNA. Translation: AAP35735.1.
AK299120 mRNA. Translation: BAH12954.1.
AK299496 mRNA. Translation: BAH13051.1.
AC025259 Genomic DNA. No translation available.
BC000254 mRNA. Translation: AAH00254.1.
BC040531 mRNA. Translation: AAH40531.1.
CCDSCCDS44893.2. [P36896-5]
CCDS44894.2. [P36896-4]
CCDS8816.1. [P36896-1]
PIRI38859.
I80182.
I80183.
RefSeqNP_004293.1. NM_004302.4. [P36896-1]
NP_064732.3. NM_020327.3. [P36896-5]
NP_064733.3. NM_020328.3. [P36896-4]
UniGeneHs.438918.

3D structure databases

ProteinModelPortalP36896.
SMRP36896. Positions 31-104, 149-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106606. 28 interactions.
DIPDIP-427N.
IntActP36896. 7 interactions.
STRING9606.ENSP00000257963.

Chemistry

BindingDBP36896.
ChEMBLCHEMBL5310.
DrugBankDB00171. Adenosine triphosphate.
GuidetoPHARMACOLOGY1787.

PTM databases

PhosphoSiteP36896.

Polymorphism databases

DMDM547775.

Proteomic databases

MaxQBP36896.
PaxDbP36896.
PRIDEP36896.

Protocols and materials databases

DNASU91.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257963; ENSP00000257963; ENSG00000135503. [P36896-1]
ENST00000415850; ENSP00000397550; ENSG00000135503. [P36896-3]
ENST00000426655; ENSP00000390477; ENSG00000135503. [P36896-2]
ENST00000541224; ENSP00000442656; ENSG00000135503. [P36896-4]
ENST00000542485; ENSP00000442885; ENSG00000135503. [P36896-5]
GeneID91.
KEGGhsa:91.
UCSCuc001rzl.3. human. [P36896-3]
uc001rzm.3. human. [P36896-2]
uc001rzn.3. human. [P36896-1]
uc010snn.2. human. [P36896-4]

Organism-specific databases

CTD91.
GeneCardsGC12P052375.
HGNCHGNC:172. ACVR1B.
HPACAB026126.
MIM601300. gene.
neXtProtNX_P36896.
PharmGKBPA24493.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000230587.
HOVERGENHBG054502.
InParanoidP36896.
KOK13567.
OMAQCACTSC.
OrthoDBEOG7Q8CN3.
PhylomeDBP36896.
TreeFamTF314724.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
SignaLinkP36896.

Gene expression databases

ArrayExpressP36896.
BgeeP36896.
CleanExHS_ACVR1B.
GenevestigatorP36896.

Family and domain databases

InterProIPR000472. 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]
PANTHERPTHR23255. PTHR23255. 1 hit.
PfamPF01064. Activin_recp. 1 hit.
PF00069. 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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiACVR1B.
GenomeRNAi91.
NextBio339.
PROP36896.
SOURCESearch...

Entry information

Entry nameACV1B_HUMAN
AccessionPrimary (citable) accession number: P36896
Secondary accession number(s): B7Z5L8 expand/collapse secondary AC list , B7Z5W5, Q15479, Q15480, Q15481, Q15482
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM