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P27037 (AVR2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Activin receptor type-2A

EC=2.7.11.30
Alternative name(s):
Activin receptor type IIA
Short name=ACTR-IIA
Short name=ACTRIIA
Gene names
Name:ACVR2A
Synonyms:ACVR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A.

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Interacts with AIP1. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentMembrane
   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
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from direct assay PubMed 18436533. Source: BHF-UCL

Sertoli cell proliferation

Inferred from electronic annotation. Source: Ensembl

activin receptor signaling pathway

Inferred from direct assay PubMed 12665502. Source: GOC

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

determination of left/right symmetry

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system development

Inferred from electronic annotation. Source: Ensembl

gastrulation with mouth forming second

Inferred from electronic annotation. Source: Ensembl

mesoderm development

Inferred from electronic annotation. Source: Ensembl

penile erection

Inferred from electronic annotation. Source: Ensembl

positive regulation of activin receptor signaling pathway

Inferred from direct assay PubMed 12665502. Source: HGNC

positive regulation of bone mineralization

Inferred from mutant phenotype PubMed 18436533. Source: BHF-UCL

positive regulation of erythrocyte differentiation

Inferred from direct assay PubMed 9032295. Source: HGNC

positive regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 18436533. Source: BHF-UCL

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from mutant phenotype PubMed 19366699. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 17472960. Source: MGI

regulation of BMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Ensembl

sperm ejaculation

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

transmembrane receptor protein serine/threonine kinase signaling pathway

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 14738881. Source: HGNC

inhibin-betaglycan-ActRII complex

Inferred from direct assay PubMed 10746731. Source: BHF-UCL

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

coreceptor activity

Inferred from direct assay PubMed 10746731. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 11266516PubMed 8242742PubMed 9032295. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from experiment. Source: Reactome

receptor signaling protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

transforming growth factor beta-activated receptor activity

Inferred from electronic annotation. Source: InterPro

transmembrane receptor protein serine/threonine kinase activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P27037-1)

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: P27037-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 513494Activin receptor type-2A
PRO_0000024398

Regions

Topological domain20 – 135116Extracellular Potential
Transmembrane136 – 16126Helical; Potential
Topological domain162 – 513352Cytoplasmic Potential
Domain192 – 485294Protein kinase
Nucleotide binding198 – 2069ATP By similarity

Sites

Active site3221Proton acceptor By similarity
Binding site2191ATP By similarity

Amino acid modifications

Glycosylation431N-linked (GlcNAc...) Potential
Glycosylation661N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 60 By similarity
Disulfide bond50 ↔ 78 By similarity
Disulfide bond85 ↔ 104 By similarity
Disulfide bond91 ↔ 103 By similarity
Disulfide bond105 ↔ 110 By similarity

Natural variations

Alternative sequence1 – 108108Missing in isoform 2.
VSP_054689
Natural variant2581S → R. Ref.10
Corresponds to variant rs34917571 [ dbSNP | Ensembl ].
VAR_032809
Natural variant3061D → N in a gastric adenocarcinoma sample; somatic mutation. Ref.10
VAR_032810
Natural variant3671A → T Found in a clear cell renal carcinoma case; somatic mutation. Ref.11
VAR_064692

Experimental info

Sequence conflict131L → V in BAA06548. Ref.4
Sequence conflict204 – 2063GCV → PSL in BAA06548. Ref.4
Sequence conflict3481E → V in BAA06548. Ref.4
Sequence conflict5071P → L in AAH67417. Ref.8

Secondary structure

.................................................. 513
Helix Strand Turn

Details...

Sequences

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

Last modified August 1, 1992. Version 1.
Checksum: A89822E880979618

FASTA51357,848
        10         20         30         40         50         60 
MGAAAKLAFA VFLISCSSGA ILGRSETQEC LFFNANWEKD RTNQTGVEPC YGDKDKRRHC 

        70         80         90        100        110        120 
FATWKNISGS IEIVKQGCWL DDINCYDRTD CVEKKDSPEV YFCCCEGNMC NEKFSYFPEM 

       130        140        150        160        170        180 
EVTQPTSNPV TPKPPYYNIL LYSLVPLMLI AGIVICAFWV YRHHKMAYPP VLVPTQDPGP 

       190        200        210        220        230        240 
PPPSPLLGLK PLQLLEVKAR GRFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEVYSLPG 

       250        260        270        280        290        300 
MKHENILQFI GAEKRGTSVD VDLWLITAFH EKGSLSDFLK ANVVSWNELC HIAETMARGL 

       310        320        330        340        350        360 
AYLHEDIPGL KDGHKPAISH RDIKSKNVLL KNNLTACIAD FGLALKFEAG KSAGDTHGQV 

       370        380        390        400        410        420 
GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELASR CTAADGPVDE YMLPFEEEIG 

       430        440        450        460        470        480 
QHPSLEDMQE VVVHKKKRPV LRDYWQKHAG MAMLCETIEE CWDHDAEARL SAGCVGERIT 

       490        500        510 
QMQRLTNIIT TEDIVTVVTM VTNVDFPPKE SSL 

« Hide

Isoform 2 [UniParc].

Checksum: F0D4F7B18BD200AB
Show »

FASTA40545,713

References

« Hide 'large scale' references
[1]"Cloning of the human activin receptor cDNA reveals high evolutionary conservation."
Matzuk M.M., Bradley A.
Biochim. Biophys. Acta 1130:105-108(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[2]"Molecular cloning and binding properties of the human type II activin receptor."
Donaldson C.J., Mathews L.S., Vale W.W.
Biochem. Biophys. Res. Commun. 184:310-316(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[3]Geiser A.G.
Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Mammary gland.
[4]Iimura T., Oida S.
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [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 1 AND 2).
Tissue: Colon and Hippocampus.
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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).
[9]"Crystal structure of activin receptor type-IIa (ACVR2A) kinase domain in complex with dorsomorphin."
Structural genomics consortium (SGC)
Submitted (FEB-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 191-488 IN COMPLEX WITH DORSOMORPHIN.
[10]"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: VARIANTS ARG-258 AND ASN-306.
[11]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-367.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63128 mRNA. Translation: CAA44839.1.
M93415 mRNA. Translation: AAA35504.1.
X62381 mRNA. Translation: CAA44245.1.
D31770 mRNA. Translation: BAA06548.1.
AK301629 mRNA. Translation: BAG63114.1.
AK314124 mRNA. Translation: BAG36815.1.
AC009480 Genomic DNA. Translation: AAX93050.1.
CH471058 Genomic DNA. Translation: EAX11561.1.
CH471058 Genomic DNA. Translation: EAX11562.1.
BC067418 mRNA. Translation: AAH67418.1.
BC067417 mRNA. Translation: AAH67417.1.
BC069707 mRNA. Translation: AAH69707.1.
CCDSCCDS33301.1.
PIRJQ1486.
RefSeqNP_001265508.1. NM_001278579.1. [P27037-1]
NP_001265509.1. NM_001278580.1. [P27037-2]
NP_001607.1. NM_001616.4. [P27037-1]
UniGeneHs.470174.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q4TX-ray1.96A/B191-488[»]
3SOCX-ray1.95A/B191-488[»]
4ASXX-ray2.05A/B191-488[»]
ProteinModelPortalP27037.
SMRP27037. Positions 26-119, 191-486.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106607. 17 interactions.
DIPDIP-520N.
IntActP27037. 1 interaction.
MINTMINT-122188.
STRING9606.ENSP00000241416.

Chemistry

BindingDBP27037.
ChEMBLCHEMBL5616.
GuidetoPHARMACOLOGY1791.

PTM databases

PhosphoSiteP27037.

Polymorphism databases

DMDM114722.

Proteomic databases

MaxQBP27037.
PaxDbP27037.
PRIDEP27037.

Protocols and materials databases

DNASU92.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000241416; ENSP00000241416; ENSG00000121989.
ENST00000404590; ENSP00000384338; ENSG00000121989.
ENST00000535787; ENSP00000439988; ENSG00000121989.
GeneID92.
KEGGhsa:92.
UCSCuc002twg.3. human. [P27037-1]

Organism-specific databases

CTD92.
GeneCardsGC02P148602.
HGNCHGNC:173. ACVR2A.
HPAHPA046997.
MIM102581. gene.
neXtProtNX_P27037.
PharmGKBPA24494.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231495.
HOVERGENHBG054502.
InParanoidP27037.
KOK04670.
OMAEDPGNWI.
OrthoDBEOG7JHM5B.
PhylomeDBP27037.
TreeFamTF352876.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
SignaLinkP27037.

Gene expression databases

ArrayExpressP27037.
BgeeP27037.
CleanExHS_ACVR2A.
GenevestigatorP27037.

Family and domain databases

InterProIPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERPTHR23255. PTHR23255. 1 hit.
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR00653. ACTIVIN2R.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP27037.
GeneWikiACVR2A.
GenomeRNAi92.
NextBio347.
PROP27037.
SOURCESearch...

Entry information

Entry nameAVR2A_HUMAN
AccessionPrimary (citable) accession number: P27037
Secondary accession number(s): B2RAB8 expand/collapse secondary AC list , B4DWQ2, D3DP85, Q53TH4, Q6NWV2, Q92474
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 155 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 2

Human chromosome 2: entries, gene names and cross-references to MIM