Interleukin-1 receptor-associated kinase 1

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Reviewed, UniProtKB/Swiss-Prot P51617 (IRAK1_HUMAN)

Last modified February 9, 2010. Version 104. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Interleukin-1 receptor-associated kinase 1
      Short name=IRAK-1
    EC=2.7.11.1

Gene names

Name:	IRAK1
Synonyms:	IRAK

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	712 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Binds to the IL-1 type I receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization. Isoform 1 binds rapidly but is then degraded allowing isoform 2 to mediate a slower, more sustained response to the cytokine. Isoform 2 is inactive suggesting that the kinase activity of this enzyme is not required for IL-1 signaling. Once phosphorylated, IRAK1 recruits the adapter protein PELI1. Ref.3 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Subunit structure	IL-1 stimulation leads to the formation of a signaling complex which dissociates from the IL-1 receptor following the binding of PELI1. Interacts with IL1RL1. Interacts with IRAK1BP1 By similarity. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10
Tissue specificity	Isoform 1 and isoform 2 are ubiquitously expressed in all tissues examined, with isoform 1 being more strongly expressed than isoform 2. Ref.3
Post-translational modification	Autophosphorylated or is transphosphorylated by IRAK4 following recruitment to the IL-1RI. In the case of isoform 1, this is linked to ubiquitination and degradation. Ref.3 Ref.11 Ref.12 Polyubiquitinated; after cell stimulation with IL-1-beta. Polyubiquitination occurs with polyubiquitin chains linked through 'Lys-63'.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Pelle subfamily. Contains 1 protein kinase domain.

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Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: UniProtKB activation of NF-kappaB-inducing kinase activity Ref.3 Inferred from direct assay. Source: UniProtKB anti-apoptosis Inferred from Experiment. Source: Reactome interleukin-1-mediated signaling pathway Inferred from mutant phenotype. Source: UniProtKB lipopolysaccharide-mediated signaling pathway Inferred from mutant phenotype. Source: UniProtKB negative regulation of NF-kappaB transcription factor activity Inferred from mutant phenotype. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from direct assay. Source: UniProtKB positive regulation of transcription Ref.3 Non-traceable author statement. Source: UniProtKB protein amino acid autophosphorylation Ref.3 Non-traceable author statement. Source: UniProtKB protein oligomerization Inferred from mutant phenotype. Source: UniProtKB regulation of cytokine-mediated signaling pathway Inferred from mutant phenotype. Source: UniProtKB response to interleukin-1 Inferred from mutant phenotype. Source: UniProtKB response to lipopolysaccharide Inferred from mutant phenotype. Source: UniProtKB toll-like receptor 2 signaling pathway Inferred from mutant phenotype. Source: UniProtKB transmembrane receptor protein serine/threonine kinase signaling pathway Ref.3 Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome interleukin-1 receptor complex Non-traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NF-kappaB-inducing kinase activity Ref.1 Traceable author statement. Source: ProtInc magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.3 Ref.7 Ref.8 Inferred from physical interaction. Source: UniProtKB protein heterodimerization activity Inferred from physical interaction. Source: UniProtKB protein homodimerization activity Ref.3 Non-traceable author statement. Source: UniProtKB transcription activator activity Ref.3 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-358664,EBI-358664
IRAK2	O43187	1	EBI-358664,EBI-447733
IRAK3	Q9Y616	1	EBI-358664,EBI-447690
MYD88	Q99836	1	EBI-358664,EBI-447677
PELI2	Q9HAT8	2	EBI-358664,EBI-448407
PELI3	Q8N2H9-1	1	EBI-487386,EBI-448466
PELI3	Q8N2H9-2	1	EBI-358664,EBI-448472
TRAF6	Q9Y4K3	3	EBI-358664,EBI-359276

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Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P51617-1) Also known as: a; 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: P51617-2) Also known as: b; The sequence of this isoform differs from the canonical sequence as follows: 513-542: Missing.
Note: Inactive.

Isoform 3 (identifier: P51617-3) The sequence of this isoform differs from the canonical sequence as follows: 45-45: F → FGGWRRAAGGREARGLLAPTPDAPRPA 478-492: Missing. 513-542: Missing.
Note: No experimental confirmation available.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 712

712

Interleukin-1 receptor-associated kinase 1

PRO_0000086030

Regions

Domain

212 – 521

310

Protein kinase

Nucleotide binding

218 – 226

ATP By similarity

Sites

Active site

340

Proton acceptor By similarity

Binding site

239

ATP

Amino acid modifications

Modified residue

131

Phosphoserine Ref.12

Modified residue

371

Phosphoserine Ref.12

Modified residue

568

Phosphoserine Ref.11

Natural variations

Alternative sequence

F → FGGWRRAAGGREARGLLAPT PDAPRPA in isoform 3.

VSP_011849

Alternative sequence

478 – 492

Missing in isoform 3.

VSP_011850

Alternative sequence

513 – 542

Missing in isoform 2 and isoform 3.

VSP_011851

Natural variant

194

R → H: dbSNP rs11465830.

VAR_051629

Natural variant

196

F → S: dbSNP rs1059702. Ref.1

VAR_051630

Natural variant

203

C → S: dbSNP rs10127175.

VAR_051631

Natural variant

398

T → M: dbSNP rs56340948. Ref.14

VAR_040573

Natural variant

412

V → M in a glioblastoma multiforme sample; somatic mutation. Ref.14

VAR_040574

Natural variant

421

Q → H in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.14

VAR_040575

Natural variant

532

S → L: dbSNP rs1059703. Ref.1 Ref.14

VAR_040576

Natural variant

619

G → S: dbSNP rs34112487. Ref.14

VAR_040577

Natural variant

625

T → M: dbSNP rs35638718. Ref.14

VAR_040578

Natural variant

638

R → W: dbSNP rs56082801. Ref.14

VAR_040579

Natural variant

690

S → G in a lung adenocarcinoma sample; somatic mutation. Ref.14

VAR_040580

Experimental info

Mutagenesis

239

K → S: Loss of kinase activity. Ref.9

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Sequences

Sequence		Length	Mass (Da)
Isoform 1 (a) [UniParc]. Last modified December 1, 2000. Version 2. Checksum: A7ADED75D3A3981D Show »	FASTA	712	76,537
10 20 30 40 50 60 MAGGPGPGEP AAPGAQHFLY EVPPWVMCRF YKVMDALEPA DWCQFAALIV RDQTELRLCE 70 80 90 100 110 120 RSGQRTASVL WPWINRNARV ADLVHILTHL QLLRARDIIT AWHPPAPLPS PGTTAPRPSS 130 140 150 160 170 180 IPAPAEAEAW SPRKLPSSAS TFLSPAFPGS QTHSGPELGL VPSPASLWPP PPSPAPSSTK 190 200 210 220 230 240 PGPESSVSLL QGARPFPFCW PLCEISRGTH NFSEELKIGE GGFGCVYRAV MRNTVYAVKR 250 260 270 280 290 300 LKENADLEWT AVKQSFLTEV EQLSRFRHPN IVDFAGYCAQ NGFYCLVYGF LPNGSLEDRL 310 320 330 340 350 360 HCQTQACPPL SWPQRLDILL GTARAIQFLH QDSPSLIHGD IKSSNVLLDE RLTPKLGDFG 370 380 390 400 410 420 LARFSRFAGS SPSQSSMVAR TQTVRGTLAY LPEEYIKTGR LAVDTDTFSF GVVVLETLAG 430 440 450 460 470 480 QRAVKTHGAR TKYLKDLVEE EAEEAGVALR STQSTLQAGL AADAWAAPIA MQIYKKHLDP 490 500 510 520 530 540 RPGPCPPELG LGLGQLACCC LHRRAKRRPP MTQVYERLEK LQAVVAGVPG HSEAASCIPP 550 560 570 580 590 600 SPQENSYVSS TGRAHSGAAP WQPLAAPSGA SAQAAEQLQR GPNQPVESDE SLGGLSAALR 610 620 630 640 650 660 SWHLTPSCPL DPAPLREAGC PQGDTAGESS WGSGPGSRPT AVEGLALGSS ASSSSEPPQI 670 680 690 700 710 IINPARQKMV QKLALYEDGA LDSLQLLSSS SLPGLGLEQD RQGPEESDEF QS « Hide
Isoform 2 (b). Checksum: 687C7EB6064FA918 Show »	FASTA	682	73,421
10 20 30 40 50 60 MAGGPGPGEP AAPGAQHFLY EVPPWVMCRF YKVMDALEPA DWCQFAALIV RDQTELRLCE 70 80 90 100 110 120 RSGQRTASVL WPWINRNARV ADLVHILTHL QLLRARDIIT AWHPPAPLPS PGTTAPRPSS 130 140 150 160 170 180 IPAPAEAEAW SPRKLPSSAS TFLSPAFPGS QTHSGPELGL VPSPASLWPP PPSPAPSSTK 190 200 210 220 230 240 PGPESSVSLL QGARPFPFCW PLCEISRGTH NFSEELKIGE GGFGCVYRAV MRNTVYAVKR 250 260 270 280 290 300 LKENADLEWT AVKQSFLTEV EQLSRFRHPN IVDFAGYCAQ NGFYCLVYGF LPNGSLEDRL 310 320 330 340 350 360 HCQTQACPPL SWPQRLDILL GTARAIQFLH QDSPSLIHGD IKSSNVLLDE RLTPKLGDFG 370 380 390 400 410 420 LARFSRFAGS SPSQSSMVAR TQTVRGTLAY LPEEYIKTGR LAVDTDTFSF GVVVLETLAG 430 440 450 460 470 480 QRAVKTHGAR TKYLKDLVEE EAEEAGVALR STQSTLQAGL AADAWAAPIA MQIYKKHLDP 490 500 510 520 530 540 RPGPCPPELG LGLGQLACCC LHRRAKRRPP MTQENSYVSS TGRAHSGAAP WQPLAAPSGA 550 560 570 580 590 600 SAQAAEQLQR GPNQPVESDE SLGGLSAALR SWHLTPSCPL DPAPLREAGC PQGDTAGESS 610 620 630 640 650 660 WGSGPGSRPT AVEGLALGSS ASSSSEPPQI IINPARQKMV QKLALYEDGA LDSLQLLSSS 670 680 SLPGLGLEQD RQGPEESDEF QS « Hide
Isoform 3. Checksum: D744A32E997E1246 Show »	FASTA	693	74,560
10 20 30 40 50 60 MAGGPGPGEP AAPGAQHFLY EVPPWVMCRF YKVMDALEPA DWCQFGGWRR AAGGREARGL 70 80 90 100 110 120 LAPTPDAPRP AAALIVRDQT ELRLCERSGQ RTASVLWPWI NRNARVADLV HILTHLQLLR 130 140 150 160 170 180 ARDIITAWHP PAPLPSPGTT APRPSSIPAP AEAEAWSPRK LPSSASTFLS PAFPGSQTHS 190 200 210 220 230 240 GPELGLVPSP ASLWPPPPSP APSSTKPGPE SSVSLLQGAR PFPFCWPLCE ISRGTHNFSE 250 260 270 280 290 300 ELKIGEGGFG CVYRAVMRNT VYAVKRLKEN ADLEWTAVKQ SFLTEVEQLS RFRHPNIVDF 310 320 330 340 350 360 AGYCAQNGFY CLVYGFLPNG SLEDRLHCQT QACPPLSWPQ RLDILLGTAR AIQFLHQDSP 370 380 390 400 410 420 SLIHGDIKSS NVLLDERLTP KLGDFGLARF SRFAGSSPSQ SSMVARTQTV RGTLAYLPEE 430 440 450 460 470 480 YIKTGRLAVD TDTFSFGVVV LETLAGQRAV KTHGARTKYL KDLVEEEAEE AGVALRSTQS 490 500 510 520 530 540 TLQAGLAADA WAAPIAMQIY KKHLGQLACC CLHRRAKRRP PMTQENSYVS STGRAHSGAA 550 560 570 580 590 600 PWQPLAAPSG ASAQAAEQLQ RGPNQPVESD ESLGGLSAAL RSWHLTPSCP LDPAPLREAG 610 620 630 640 650 660 CPQGDTAGES SWGSGPGSRP TAVEGLALGS SASSSSEPPQ IIINPARQKM VQKLALYEDG 670 680 690 ALDSLQLLSS SSLPGLGLEQ DRQGPEESDE FQS « Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"IRAK: a kinase associated with the interleukin-1 receptor." Cao Z., Henzel W.J., Gao X. Science 271:1128-1131(1996) [PubMed: 8599092] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANTS SER-196 AND LEU-532.
[2]	"Comparative sequence analysis of the MECP2-locus in human and mouse reveals new transcribed regions." Reichwald K., Thiesen J., Wiehe T., Weitzel J., Poustka W.A., Rosenthal A., Platzer M., Stratling W.H., Kioschis P. Mamm. Genome 11:182-190(2000) [PubMed: 10723722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[3]	"IRAK1b, a novel alternative splice variant of interleukin-1 receptor-associated kinase (IRAK), mediates interleukin-1 signaling and has prolonged stability." Jensen L.E., Whitehead A.S. J. Biol. Chem. 276:29037-29044(2001) [PubMed: 11397809] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Placenta.
[5]	"IRAK4: a novel member of the IRAK family with the properties of an IRAK-kinase." Li S., Strelow A., Fontana E.J., Wesche H. Proc. Natl. Acad. Sci. U.S.A. 99:5567-5572(2002) [PubMed: 11960013] [Abstract] Cited for: INTERACTION WITH IRAK4.
[6]	"Pellino 1 is required for interleukin-1 (IL-1)-mediated signaling through its interaction with the IL-1 receptor-associated kinase 4 (IRAK4)-IRAK-tumor necrosis factor receptor-associated factor 6 (TRAF6) complex." Jiang Z., Johnson H.J., Nie H., Qin J., Bird T.A., Li X. J. Biol. Chem. 278:10952-10956(2003) [PubMed: 12496252] [Abstract] Cited for: INTERACTION WITH PELI1.
[7]	"Characterization of Pellino2, a substrate of IRAK1 and IRAK4." Strelow A., Kollewe C., Wesche H. FEBS Lett. 547:157-161(2003) [PubMed: 12860405] [Abstract] Cited for: INTERACTION WITH PELI2.
[8]	"Pellino3, a novel member of the Pellino protein family, promotes activation of c-Jun and Elk-1 and may act as a scaffolding protein." Jensen L.E., Whitehead A.S. J. Immunol. 171:1500-1506(2003) [PubMed: 12874243] [Abstract] Cited for: INTERACTION WITH PELI3.
[9]	"IRAK4 kinase activity is redundant for interleukin-1 (IL-1) receptor-associated kinase phosphorylation and IL-1 responsiveness." Qin J., Jiang Z., Qian Y., Casanova J.-L., Li X. J. Biol. Chem. 279:26748-26753(2004) [PubMed: 15084582] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-239.
[10]	"IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST 2 and induces T helper type 2-associated cytokines." Schmitz J., Owyang A., Oldham E., Song Y., Murphy E., McClanahan T.K., Zurawski G., Moshrefi M., Qin J., Li X., Gorman D.M., Bazan J.F., Kastelein R.A. Immunity 23:479-490(2005) [PubMed: 16286016] [Abstract] Cited for: INTERACTION WITH IL1RL1.
[11]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568, MASS SPECTROMETRY. Tissue: T-cell.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-371, MASS SPECTROMETRY.
[13]	"Direct activation of protein kinases by unanchored polyubiquitin chains." Xia Z.-P., Sun L., Chen X., Pineda G., Jiang X., Adhikari A., Zeng W., Chen Z.J. Nature 461:114-119(2009) [PubMed: 19675569] [Abstract] Cited for: UBIQUITINATION.
[14]	"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. Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-398; MET-412; HIS-421; LEU-532; SER-619; MET-625; TRP-638 AND GLY-690.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	L76191 mRNA. Translation: AAC41949.1. U52112 Genomic DNA. No translation available. AF030876 Genomic DNA. Translation: AAC08756.1. AF346607 mRNA. Translation: AAK62888.1. BC054000 mRNA. Translation: AAH54000.1.
IPI	IPI00293652. IPI00472717. IPI00940703.
PIR	G02512.
RefSeq	NP_001020413.1. NP_001020414.1. NP_001560.2.
UniGene	Hs.522819
3D structure databases
SMR	P51617. Positions 16-124.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-397N.
IntAct	P51617. 14 interactions.
STRING	P51617.
PTM databases
PhosphoSite	P51617.
Proteomic databases
PRIDE	P51617.
Genome annotation databases
Ensembl	ENST00000369980; ENSP00000358997; ENSG00000184216; Homo sapiens. [Genome view]
GeneID	3654.
KEGG	hsa:3654.
UCSC	uc004fjr.1. human. uc004fjs.1. human.
Organism-specific databases
CTD	3654.
GeneCards	GC0XM152929.
H-InvDB	HIX0017146.
HGNC	HGNC:6112. IRAK1.
HPA	CAB004461.
MIM	300283. gene.
PharmGKB	PA29912.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16552.
HOGENOM	HBG283634.
HOVERGEN	P51617.
InParanoid	P51617.
OMA	WHLTPSC.
OrthoDB	EOG9NS5XG.
PhylomeDB	P51617.
Enzyme and pathway databases
BRENDA	2.7.10.2. 247. 2.7.11.1. 247.
Pathway_Interaction_DB	il1pathway. IL1-mediated signaling events. p75ntrpathway. p75(NTR)-mediated signaling.
Reactome	REACT_11061. Signalling by NGF. REACT_6900. Signaling in Immune system.
Gene expression databases
ArrayExpress	P51617.
Bgee	P51617.
CleanEx	HS_IRAK1.
Genevestigator	P51617.
GermOnline	ENSG00000184216. Homo sapiens.
Family and domain databases
InterPro	IPR000488. Death. IPR011029. DEATH-like. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. [Graphical view]
Pfam	PF00531. Death. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	14289.
SOURCE	Search...

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Entry information

Entry name

IRAK1_HUMAN

Accession

Primary (citable) accession number: P51617
Secondary accession number(s): Q7Z5V4, Q96RL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 1, 2000
Last modified:	February 9, 2010
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

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