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Q13705

- AVR2B_HUMAN

UniProt

Q13705 - AVR2B_HUMAN

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Protein
Activin receptor type-2B
Gene
ACVR2B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 2171ATP By similarity
Active sitei321 – 3211Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2049ATP By similarity

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 kinase activity Source: HGNC
  6. protein serine/threonine/tyrosine kinase activity Source: Ensembl
  7. receptor signaling protein serine/threonine kinase activity Source: InterPro
  8. transforming growth factor beta-activated receptor activity Source: InterPro

GO - Biological processi

  1. BMP signaling pathway Source: BHF-UCL
  2. activation of protein kinase activity Source: Ensembl
  3. activin receptor signaling pathway Source: GOC
  4. anterior/posterior pattern specification Source: HGNC
  5. artery development Source: BHF-UCL
  6. blood vessel remodeling 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 137119Extracellular Reviewed prediction
Add
BLAST
Transmembranei138 – 15821Helical; Reviewed prediction
Add
BLAST
Topological domaini159 – 512354Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 512494Activin receptor type-2B
PRO_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 VPS39.2 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

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.

Miscellaneous databases

EvolutionaryTraceiQ13705.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini190 – 480291Protein kinase
Add
BLAST

Sequence similaritiesi

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):

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 172CA → WP in CAA54671. 1 Publication
Sequence conflicti64 – 641R → A1 Publication
Sequence conflicti64 – 641R → A1 Publication
Sequence conflicti459 – 4591E → A in AAC64515. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 156 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

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