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Q9NZN1

- IRPL1_HUMAN

UniProt

Q9NZN1 - IRPL1_HUMAN

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Protein

Interleukin-1 receptor accessory protein-like 1

Gene

IL1RAPL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in presynaptic and postsynaptic differentiation and dendritic spine formation in neurons.2 Publications

GO - Molecular functioni

  1. receptor binding Source: BHF-UCL
  2. voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  1. calcium ion transmembrane transport Source: GOC
  2. heterophilic cell-cell adhesion Source: BHF-UCL
  3. negative regulation of exocytosis Source: UniProtKB
  4. neuron differentiation Source: BHF-UCL
  5. positive regulation of dendrite morphogenesis Source: BHF-UCL
  6. presynaptic membrane assembly Source: BHF-UCL
  7. regulation of neuron projection development Source: UniProtKB
  8. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-1 receptor accessory protein-like 1
Short name:
IL-1-RAPL-1
Short name:
IL-1RAPL-1
Short name:
IL1RAPL-1
Alternative name(s):
Oligophrenin-4
Three immunoglobulin domain-containing IL-1 receptor-related 2
Short name:
TIGIRR-2
X-linked interleukin-1 receptor accessory protein-like 1
Gene namesi
Name:IL1RAPL1
Synonyms:OPHN4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:5996. IL1RAPL1.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cytoplasm 1 Publication. Cell projectionaxon By similarity. Cell projectiondendrite By similarity
Note: May localize to the cell body and growth cones of dendrite-like processes.By similarity

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. cytoplasm Source: UniProtKB-KW
  3. dendrite Source: BHF-UCL
  4. integral component of membrane Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB
  6. postsynaptic membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked 21 (MRX21) [MIM:300143]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi300143. phenotype.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA29812.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 696678Interleukin-1 receptor accessory protein-like 1PRO_0000015454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 118PROSITE-ProRule annotation
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi164 ↔ 216PROSITE-ProRule annotation
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi267 ↔ 334PROSITE-ProRule annotation
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9NZN1.
PaxDbiQ9NZN1.
PeptideAtlasiQ9NZN1.
PRIDEiQ9NZN1.

PTM databases

PhosphoSiteiQ9NZN1.

Expressioni

Tissue specificityi

Detected at low levels in heart, skeletal muscle, ovary, skin, amygdala, caudate nucleus, corpus callosum, hippocampus, substantia nigra and thalamus. Detected at very low levels in tonsil, prostate, testis, small intestine, placenta, colon and fetal liver.2 Publications

Gene expression databases

BgeeiQ9NZN1.
CleanExiHS_IL1RAPL1.
ExpressionAtlasiQ9NZN1. baseline and differential.
GenevestigatoriQ9NZN1.

Organism-specific databases

HPAiHPA000564.

Interactioni

Subunit structurei

Homodimer. Interacts (calcium-independent) with NCS1. Interacts (via extracellular region) with PTPRD; this interaction is required for IL1RAPL1-mediated synapse formation.1 Publication

Protein-protein interaction databases

BioGridi116313. 2 interactions.
IntActiQ9NZN1. 1 interaction.
STRINGi9606.ENSP00000305200.

Structurei

Secondary structure

1
696
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi405 – 4106Combined sources
Helixi426 – 4316Combined sources
Helixi433 – 4408Combined sources
Helixi449 – 4524Combined sources
Helixi459 – 46810Combined sources
Beta strandi470 – 4778Combined sources
Helixi479 – 4835Combined sources
Turni484 – 4874Combined sources
Helixi488 – 4925Combined sources
Helixi494 – 5018Combined sources
Beta strandi504 – 5118Combined sources
Helixi518 – 52912Combined sources
Beta strandi532 – 5387Combined sources
Helixi542 – 5454Combined sources
Beta strandi546 – 5483Combined sources
Helixi550 – 5589Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3GX-ray2.30A/B403-561[»]
4M92X-ray1.60B207-222[»]
ProteinModelPortaliQ9NZN1.
SMRiQ9NZN1. Positions 31-349, 403-561.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZN1.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 357339ExtracellularSequence AnalysisAdd
BLAST
Topological domaini379 – 696318CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei358 – 37821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 134116Ig-like C2-type 1Add
BLAST
Domaini143 – 23290Ig-like C2-type 2Add
BLAST
Domaini242 – 350109Ig-like C2-type 3Add
BLAST
Domaini403 – 562160TIRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni549 – 64496Interaction with NCS1Add
BLAST

Sequence similaritiesi

Belongs to the interleukin-1 receptor family.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG41227.
HOGENOMiHOG000092977.
HOVERGENiHBG052148.
InParanoidiQ9NZN1.
KOiK05170.
OMAiKLLHPLE.
OrthoDBiEOG7CVPXJ.
PhylomeDBiQ9NZN1.
TreeFamiTF333913.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.40.50.10140. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR015621. IL-1_rcpt_fam.
IPR000157. TIR_dom.
[Graphical view]
PANTHERiPTHR11890. PTHR11890. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52200. SSF52200. 1 hit.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced.

Isoform 1 (identifier: Q9NZN1-1) [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

        10         20         30         40         50
MKAPIPHLIL LYATFTQSLK VVTKRGSADG CTDWSIDIKK YQVLVGEPVR
60 70 80 90 100
IKCALFYGYI RTNYSLAQSA GLSLMWYKSS GPGDFEEPIA FDGSRMSKEE
110 120 130 140 150
DSIWFRPTLL QDSGLYACVI RNSTYCMKVS ISLTVGENDT GLCYNSKMKY
160 170 180 190 200
FEKAELSKSK EISCRDIEDF LLPTREPEIL WYKECRTKTW RPSIVFKRDT
210 220 230 240 250
LLIREVREDD IGNYTCELKY GGFVVRRTTE LTVTAPLTDK PPKLLYPMES
260 270 280 290 300
KLTIQETQLG DSANLTCRAF FGYSGDVSPL IYWMKGEKFI EDLDENRVWE
310 320 330 340 350
SDIRILKEHL GEQEVSISLI VDSVEEGDLG NYSCYVENGN GRRHASVLLH
360 370 380 390 400
KRELMYTVEL AGGLGAILLL LVCLVTIYKC YKIEIMLFYR NHFGAEELDG
410 420 430 440 450
DNKDYDAYLS YTKVDPDQWN QETGEEERFA LEILPDMLEK HYGYKLFIPD
460 470 480 490 500
RDLIPTGTYI EDVARCVDQS KRLIIVMTPN YVVRRGWSIF ELETRLRNML
510 520 530 540 550
VTGEIKVILI ECSELRGIMN YQEVEALKHT IKLLTVIKWH GPKCNKLNSK
560 570 580 590 600
FWKRLQYEMP FKRIEPITHE QALDVSEQGP FGELQTVSAI SMAAATSTAL
610 620 630 640 650
ATAHPDLRST FHNTYHSQMR QKHYYRSYEY DVPPTGTLPL TSIGNQHTYC
660 670 680 690
NIPMTLINGQ RPQTKSSREQ NPDEAHTNSA ILPLLPRETS ISSVIW
Length:696
Mass (Da):79,969
Last modified:August 22, 2003 - v2
Checksum:i9B7A0B503D73CCA9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti379 – 3791K → R.1 Publication
Corresponds to variant rs138267399 [ dbSNP | Ensembl ].
VAR_062263
Natural varianti618 – 6181Q → H.1 Publication
VAR_062264
Natural varianti637 – 6371T → S.1 Publication
VAR_062265
Natural varianti643 – 6431I → V.1 Publication
VAR_062266

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ243874 mRNA. Translation: CAB56046.1.
AF181284 mRNA. Translation: AAF59411.1.
AF284435 mRNA. Translation: AAG21369.1.
AB102650 mRNA. Translation: BAC81119.1.
AL031575
, AC005748, AC121343, AC129852, AL031466 Genomic DNA. Translation: CAI42035.1.
AL031466
, AC005748, AC121343, AC129852, AL031575 Genomic DNA. Translation: CAI42992.1.
CH471074 Genomic DNA. Translation: EAW99046.1.
BC126345 mRNA. Translation: AAI26346.1.
BC126347 mRNA. Translation: AAI26348.1.
CCDSiCCDS14218.1. [Q9NZN1-1]
RefSeqiNP_055086.1. NM_014271.3. [Q9NZN1-1]
XP_005274498.1. XM_005274441.1. [Q9NZN1-1]
UniGeneiHs.658912.

Genome annotation databases

EnsembliENST00000378993; ENSP00000368278; ENSG00000169306. [Q9NZN1-1]
GeneIDi11141.
KEGGihsa:11141.
UCSCiuc004dby.2. human. [Q9NZN1-1]

Polymorphism databases

DMDMi34222654.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ243874 mRNA. Translation: CAB56046.1 .
AF181284 mRNA. Translation: AAF59411.1 .
AF284435 mRNA. Translation: AAG21369.1 .
AB102650 mRNA. Translation: BAC81119.1 .
AL031575
, AC005748 , AC121343 , AC129852 , AL031466 Genomic DNA. Translation: CAI42035.1 .
AL031466
, AC005748 , AC121343 , AC129852 , AL031575 Genomic DNA. Translation: CAI42992.1 .
CH471074 Genomic DNA. Translation: EAW99046.1 .
BC126345 mRNA. Translation: AAI26346.1 .
BC126347 mRNA. Translation: AAI26348.1 .
CCDSi CCDS14218.1. [Q9NZN1-1 ]
RefSeqi NP_055086.1. NM_014271.3. [Q9NZN1-1 ]
XP_005274498.1. XM_005274441.1. [Q9NZN1-1 ]
UniGenei Hs.658912.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1T3G X-ray 2.30 A/B 403-561 [» ]
4M92 X-ray 1.60 B 207-222 [» ]
ProteinModelPortali Q9NZN1.
SMRi Q9NZN1. Positions 31-349, 403-561.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116313. 2 interactions.
IntActi Q9NZN1. 1 interaction.
STRINGi 9606.ENSP00000305200.

PTM databases

PhosphoSitei Q9NZN1.

Polymorphism databases

DMDMi 34222654.

Proteomic databases

MaxQBi Q9NZN1.
PaxDbi Q9NZN1.
PeptideAtlasi Q9NZN1.
PRIDEi Q9NZN1.

Protocols and materials databases

DNASUi 11141.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378993 ; ENSP00000368278 ; ENSG00000169306 . [Q9NZN1-1 ]
GeneIDi 11141.
KEGGi hsa:11141.
UCSCi uc004dby.2. human. [Q9NZN1-1 ]

Organism-specific databases

CTDi 11141.
GeneCardsi GC0XP028605.
HGNCi HGNC:5996. IL1RAPL1.
HPAi HPA000564.
MIMi 300143. phenotype.
300206. gene.
neXtProti NX_Q9NZN1.
Orphaneti 777. X-linked non-syndromic intellectual disability.
PharmGKBi PA29812.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41227.
HOGENOMi HOG000092977.
HOVERGENi HBG052148.
InParanoidi Q9NZN1.
KOi K05170.
OMAi KLLHPLE.
OrthoDBi EOG7CVPXJ.
PhylomeDBi Q9NZN1.
TreeFami TF333913.

Miscellaneous databases

ChiTaRSi IL1RAPL1. human.
EvolutionaryTracei Q9NZN1.
GeneWikii IL1RAPL1.
GenomeRNAii 11141.
NextBioi 42348.
PROi Q9NZN1.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZN1.
CleanExi HS_IL1RAPL1.
ExpressionAtlasi Q9NZN1. baseline and differential.
Genevestigatori Q9NZN1.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
3.40.50.10140. 1 hit.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR015621. IL-1_rcpt_fam.
IPR000157. TIR_dom.
[Graphical view ]
PANTHERi PTHR11890. PTHR11890. 1 hit.
Pfami PF07679. I-set. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view ]
SUPFAMi SSF52200. SSF52200. 1 hit.
PROSITEi PS50835. IG_LIKE. 3 hits.
PS50104. TIR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN NONSPECIFIC XLMR, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
    Tissue: Fetal brain.
  2. "Two novel members of the interleukin-1 receptor gene family, one deleted in Xp22.3-Xp21.3 mental retardation."
    Jin H., Gardner R.J., Viswesvaraiah R., Muntoni F., Roberts R.G.
    Eur. J. Hum. Genet. 8:87-94(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN MRX21.
  3. "Identification and characterization of two members of a novel class of the interleukin-1 receptor (IL-1R) family. Delineation of a new class of IL-1R-related proteins based on signaling."
    Born T.L., Smith D.E., Garka K.E., Renshaw B.R., Bertles J.S., Sims J.E.
    J. Biol. Chem. 275:29946-29954(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain and Testis.
  4. "Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees."
    Kitano T., Schwarz C., Nickel B., Paeaebo S.
    Mol. Biol. Evol. 20:1281-1289(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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].
    Tissue: Brain.
  8. "IL1 receptor accessory protein like, a protein involved in X-linked mental retardation, interacts with Neuronal Calcium Sensor-1 and regulates exocytosis."
    Bahi N., Friocourt G., Carrie A., Graham M.E., Weiss J.L., Chafey P., Fauchereau F., Burgoyne R.D., Chelly J.
    Hum. Mol. Genet. 12:1415-1425(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NCS1.
  9. "A truncating mutation in the IL1RAPL1 gene is responsible for X-linked mental retardation in the MRX21 family."
    Tabolacci E., Pomponi M.G., Pietrobono R., Terracciano A., Chiurazzi P., Neri G.
    Am. J. Med. Genet. A 140:482-487(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRX21.
  10. Cited for: VARIANTS ARG-379; HIS-618; SER-637 AND VAL-643.
  11. "Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL."
    Khan J.A., Brint E.K., O'Neill L.A.J., Tong L.
    J. Biol. Chem. 279:31664-31670(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 403-561, FUNCTION, DIMERIZATION.

Entry informationi

Entry nameiIRPL1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZN1
Secondary accession number(s): A0AVG4, Q9UJ53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: October 29, 2014
This is version 130 of the entry and version 2 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 X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

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