P36896 (ACV1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
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 component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Glycoprotein Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from direct assay PubMed 11117535. Source: HGNC central nervous system development Inferred from electronic annotation. Source: Compara development of primary female sexual characteristics Inferred from electronic annotation. Source: Compara hair follicle development Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara induction of apoptosis Inferred from mutant phenotype PubMed 9884026. Source: HGNC 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: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara 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 regulation of transcription, DNA-dependent Inferred from direct assay Ref.17Ref.8. Source: HGNC
Cellular_component	cell surface Inferred from direct assay Ref.17. Source: HGNC integral to plasma membrane Inferred from direct assay Ref.9. Source: HGNC
Molecular_function	ATP 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor signaling protein serine/threonine kinase activity Inferred from electronic annotation. Source: Compara transforming growth factor beta-activated receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AB1	P08238	2	EBI-1384128,EBI-352572

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 505	482	Activin receptor type-1B		PRO_0000024417
Regions
	Topological domain	24 – 126	103	Extracellular Potential
	Transmembrane	127 – 149	23	Helical; Potential
	Topological domain	150 – 505	356	Cytoplasmic Potential
	Domain	177 – 206	30	GS
	Domain	207 – 497	291	Protein kinase
	Nucleotide binding	213 – 221	9	ATP By similarity
Sites
	Active site	335	1	Proton acceptor By similarity
	Binding site	234	1	ATP By similarity
Amino acid modifications
	Modified residue	380	1	Phosphotyrosine Ref.15
	Glycosylation	43	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 52	52	Missing in isoform 5.		VSP_041841
	Alternative sequence	271	1	D → ADCSFLTLPWEVVMVSAAPK LRSLRLQYKGGRGRARFLFP LN in isoform 4.		VSP_041842
	Alternative sequence	422 – 505	84	VHEEY…EDVKI → TFLFCLCSYLPFQDAGSPKA VLLPPFFLQPVGCLLPEPES SFKVAIKGVEVAVLRVRLFF RDQFVE in isoform 3.		VSP_004953
	Alternative sequence	465 – 505	41	ALRVM…EDVKI → VRSWPPAAFPSA in isoform 2.		VSP_004954
	Natural variant	146	1	F → L. Ref.22 Corresponds to variant rs34488074 [ dbSNP | Ensembl ].		VAR_041406
	Natural variant	408	1	L → V. Corresponds to variant rs928906 [ dbSNP | Ensembl ].		VAR_011716
Isoform 3:
	Natural variant	478	1	R → H.
Experimental info
	Mutagenesis	40	1	L → A: Increases binding to activin. Ref.17
	Mutagenesis	70	1	I → A: Decreases binding to activin. Ref.17
	Mutagenesis	73	1	V → A: Increases binding to activin. Ref.17
	Mutagenesis	75	1	L → A: Decreases binding to activin. Ref.17
	Mutagenesis	77	1	P → A: Decreases binding to activin. Ref.17
	Mutagenesis	206	1	T → V: Leads to constitutive activation. Ref.8
	Sequence conflict	56	1	I → F in AAA60555. Ref.3
	Sequence conflict	56	1	I → F in AAA60556. Ref.3
	Sequence conflict	222 – 223	2	WR → MA in AAA60555. Ref.3
	Sequence conflict	222 – 223	2	WR → MA in AAA60556. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SKR2-1) [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 40A6C65CAA4C7573	FASTA	505	56,807
	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
	Isoform 2 (SKR2-2) [UniParc]. Checksum: 13269BD6D04F39D3	FASTA	476	53,411
	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 GVHEEYQLPY YDLVPSDPSI EEMRKVVCDQ KLRPNIPNWW QSYEVRSWPP AAFPSA
	Isoform 3 (SKR2-3) [UniParc]. Checksum: 969525A044E8F7C6	FASTA	487	54,270
	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 GTFLFCLCSY LPFQDAGSPK AVLLPPFFLQ PVGCLLPEPE SSFKVAIKGV EVAVLRVRLF FRDQFVE
	Isoform 4 [UniParc]. Checksum: 0A75C7D6FE406EB3	FASTA	546	61,439
	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 ADCSFLTLPW EVVMVSAAPK LRSLRLQYKG 310 320 330 340 350 360 GRGRARFLFP LNNGTWTQLW LVSDYHEHGS LFDYLNRYTV TIEGMIKLAL SAASGLAHLH 370 380 390 400 410 420 MEIVGTQGKP GIAHRDLKSK NILVKKNGMC AIADLGLAVR HDAVTDTIDI APNQRVGTKR 430 440 450 460 470 480 YMAPEVLDET INMKHFDSFK CADIYALGLV YWEIARRCNS GGVHEEYQLP YYDLVPSDPS 490 500 510 520 530 540 IEEMRKVVCD QKLRPNIPNW WQSYEALRVM GKMMRECWYA NGAARLTALR IKKTLSQLSV QEDVKI
	Isoform 5 [UniParc]. Checksum: 8E6885B168A1B026	FASTA	453	51,725
	10 20 30 40 50 60 MVSIFNLDGM EHHVRTCIPK VELVPAGKPF YCLSSEDLRN THCCYTDYCN RIDLRVPSGH 70 80 90 100 110 120 LKEPEHPSMW GPVELVGIIA GPVFLLFLII IIVFLVINYH QRVYHNRQRL DMEDPSCEMC 130 140 150 160 170 180 LSKDKTLQDL VYDLSTSGSG SGLPLFVQRT VARTIVLQEI IGKGRFGEVW RGRWRGGDVA 190 200 210 220 230 240 VKIFSSREER SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD 250 260 270 280 290 300 YLNRYTVTIE GMIKLALSAA SGLAHLHMEI VGTQGKPGIA HRDLKSKNIL VKKNGMCAIA 310 320 330 340 350 360 DLGLAVRHDA VTDTIDIAPN QRVGTKRYMA PEVLDETINM KHFDSFKCAD IYALGLVYWE 370 380 390 400 410 420 IARRCNSGGV HEEYQLPYYD LVPSDPSIEE MRKVVCDQKL RPNIPNWWQS YEALRVMGKM 430 440 450 MRECWYANGA ARLTALRIKK TLSQLSVQED VKI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[22]	"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] 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.
IPI	IPI00005732. IPI00218980. IPI00297220.
PIR	I38859. I80182. I80183.
RefSeq	NP_004293.1. NM_004302.4. NP_064732.3. NM_020327.3. NP_064733.3. NM_020328.3.
UniGene	Hs.438918.
3D structure databases
ProteinModelPortal	P36896.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-427N.
IntAct	P36896. 5 interactions.
STRING	9606.ENSP00000257963.
PTM databases
PhosphoSite	P36896.
Polymorphism databases
DMDM	547775.
Proteomic databases
PaxDb	P36896.
PRIDE	P36896.
Protocols and materials databases
DNASU	91.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000257963; ENSP00000257963; ENSG00000135503. ENST00000415850; ENSP00000397550; ENSG00000135503. ENST00000426655; ENSP00000390477; ENSG00000135503. ENST00000541224; ENSP00000442656; ENSG00000135503. ENST00000542485; ENSP00000442885; ENSG00000135503. ENST00000563546; ENSP00000456299; ENSG00000135503.
GeneID	91.
KEGG	hsa:91.
UCSC	uc001rzl.3. human. uc001rzm.3. human. uc001rzn.3. human. uc010snn.2. human.
Organism-specific databases
CTD	91.
GeneCards	GC12P052375.
HGNC	HGNC:172. ACVR1B.
MIM	601300. gene.
neXtProt	NX_P36896.
PharmGKB	PA24493.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000230587.
HOVERGEN	HBG054502.
InParanoid	P36896.
KO	K13567.
OMA	HHQRVYH.
OrthoDB	EOG4FJ88P.
PhylomeDB	P36896.
Enzyme and pathway databases
BRENDA	2.7.10.2. 2681.
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction.
SignaLink	P36896.
Gene expression databases
ArrayExpress	P36896.
Bgee	P36896.
CleanEx	HS_ACVR1B.
Genevestigator	P36896.
Family and domain databases
InterPro	IPR000472. Activin_rcpt. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_kinase_AS. IPR003605. TGF_beta_rcpt_GS. [Graphical view]
Pfam	PF01064. Activin_recp. 1 hit. PF00069. Pkinase. 1 hit. PF08515. TGF_beta_GS. 1 hit. [Graphical view]
SMART	SM00467. GS. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51256. GS. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P36896.
ChEMBL	CHEMBL5310.
DrugBank	DB00171. Adenosine triphosphate.
GenomeRNAi	91.
NextBio	339.
SOURCE	Search...

Entry information

Entry name

ACV1B_HUMAN

Accession

Primary (citable) accession number: P36896
Secondary accession number(s): B7Z5L8 , B7Z5W5, Q15479, Q15480, Q15481, Q15482

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 29, 2013
This is version 154 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.