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Protein

Leucine-rich repeat protein 1

Gene

LRR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May negatively regulate the 4-1BB-mediated signaling cascades which result in the activation of NK-kappaB and JNK1. Probable substrate recognition subunit of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat protein 1
Alternative name(s):
4-1BB-mediated-signaling molecule
4-1BBlrr
LRR-repeat protein 1
Short name:
LRR-1
Peptidylprolyl isomerase-like 5
Gene namesi
Name:LRR1
Synonyms:PPIL5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:19742. LRR1.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi341 – 3444HIIP → AAA: Abolishes interaction with CUL2 and RBX1. 1 Publication

Organism-specific databases

PharmGKBiPA134915321.

Polymorphism and mutation databases

BioMutaiLRR1.
DMDMi37079896.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Leucine-rich repeat protein 1PRO_0000084447Add
BLAST

Proteomic databases

EPDiQ96L50.
MaxQBiQ96L50.
PaxDbiQ96L50.
PRIDEiQ96L50.

PTM databases

iPTMnetiQ96L50.
PhosphoSiteiQ96L50.

Expressioni

Tissue specificityi

Ubiquitous. Maximal expression was seen in the heart and skeletal muscle and minimal expression seen in the kidney.

Gene expression databases

BgeeiQ96L50.
CleanExiHS_PPIL5.
ExpressionAtlasiQ96L50. baseline and differential.
GenevisibleiQ96L50. HS.

Interactioni

Subunit structurei

Interacts with the cytoplasmic domain of TNFRSF9. Component of the probable ECS(LRR1) E3 ubiquitin-protein ligase complex which contains CUL2, RBX1, Elongin BC complex and LRR1. Interacts with CUL2, RBX1, TCEB1 and TCEB2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MTUS2Q5JR593EBI-2510106,EBI-742948
PNMA2Q9UL423EBI-2510106,EBI-302355
TRIP13Q156453EBI-2510106,EBI-358993

Protein-protein interaction databases

BioGridi125793. 26 interactions.
IntActiQ96L50. 15 interactions.
STRINGi9606.ENSP00000298288.

Structurei

3D structure databases

ProteinModelPortaliQ96L50.
SMRiQ96L50. Positions 115-304.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati155 – 17622LRR 1Add
BLAST
Repeati178 – 19922LRR 2Add
BLAST
Repeati201 – 22222LRR 3Add
BLAST
Repeati227 – 24822LRR 4Add
BLAST
Repeati250 – 27122LRR 5Add
BLAST
Repeati273 – 29422LRR 6Add
BLAST
Repeati295 – 31622LRR 7Add
BLAST

Sequence similaritiesi

Contains 7 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00530000063533.
HOGENOMiHOG000273865.
HOVERGENiHBG045576.
InParanoidiQ96L50.
KOiK10348.
OMAiKTCVCGR.
OrthoDBiEOG7KQ229.
PhylomeDBiQ96L50.
TreeFamiTF319257.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF12799. LRR_4. 1 hit.
PF13516. LRR_6. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 4 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96L50-1) [UniParc]FASTAAdd to basket

Also known as: LRR-1a

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
MKLHCEVEVI SRHLPALGLR NRGKGVRAVL SLCQQTSRSQ PPVRAFLLIS
60 70 80 90 100
TLKDKRGTRY ELRENIEQFF TKFVDEGKAT VRLKEPPVDI CLSKAISSSL
110 120 130 140 150
KGFLSAMRLA HRGCNVDTPV STLTPVKTSE FENFKTKMVI TSKKDYPLSK
160 170 180 190 200
NFPYSLEHLQ TSYCGLVRVD MRMLCLKSLR KLDLSHNHIK KLPATIGDLI
210 220 230 240 250
HLQELNLNDN HLESFSVALC HSTLQKSLRS LDLSKNKIKA LPVQFCQLQE
260 270 280 290 300
LKNLKLDDNE LIQFPCKIGQ LINLRFLSAA RNKLPFLPSE FRNLSLEYLD
310 320 330 340 350
LFGNTFEQPK VLPVIKLQAP LTLLESSART ILHNRIPYGS HIIPFHLCQD
360 370 380 390 400
LDTAKICVCG RFCLNSFIQG TTTMNLHSVA HTVVLVDNLG GTEAPIISYF
410
CSLGCYVNSS DMLK
Length:414
Mass (Da):46,723
Last modified:September 26, 2003 - v2
Checksum:iB19B178D6CB33C4C
GO
Isoform 2 (identifier: Q96L50-2) [UniParc]FASTAAdd to basket

Also known as: LRR-1b

The sequence of this isoform differs from the canonical sequence as follows:
     95-146: AISSSLKGFL...KMVITSKKDY → DSIWLSYHSI...FCCPHCGLSR
     147-414: Missing.

Show »
Length:146
Mass (Da):16,964
Checksum:i2D91A9E05740A5C2
GO

Sequence cautioni

The sequence CAD62625.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91V → A in BAG56701 (PubMed:14702039).Curated
Sequence conflicti25 – 251G → V in AAL11430 (PubMed:11804328).Curated
Sequence conflicti28 – 281A → S in AAL11430 (PubMed:11804328).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961I → N.
Corresponds to variant rs17121605 [ dbSNP | Ensembl ].
VAR_051095
Natural varianti229 – 2291R → W.
Corresponds to variant rs7148147 [ dbSNP | Ensembl ].
VAR_051096

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei95 – 14652AISSS…SKKDY → DSIWLSYHSIPSLPRFGYRK NLCLWKILSELFHSRNYYHE SAFCCPHCGLSR in isoform 2. 2 PublicationsVSP_008363Add
BLAST
Alternative sequencei147 – 414268Missing in isoform 2. 2 PublicationsVSP_008364Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY052405 mRNA. Translation: AAL11430.1.
BX248298 mRNA. Translation: CAD62625.1. Different initiation.
AK293156 mRNA. Translation: BAG56701.1.
CH471078 Genomic DNA. Translation: EAW65761.1.
BC030142 mRNA. Translation: AAH30142.1.
BC093697 mRNA. Translation: AAH93697.1.
BC112241 mRNA. Translation: AAI12242.1.
BC139921 mRNA. Translation: AAI39922.1.
CCDSiCCDS9686.1. [Q96L50-1]
CCDS9687.1. [Q96L50-2]
RefSeqiNP_689542.2. NM_152329.3. [Q96L50-1]
NP_982292.1. NM_203467.1. [Q96L50-2]
UniGeneiHs.451090.

Genome annotation databases

EnsembliENST00000298288; ENSP00000298288; ENSG00000165501. [Q96L50-1]
ENST00000318317; ENSP00000315628; ENSG00000165501. [Q96L50-2]
GeneIDi122769.
KEGGihsa:122769.
UCSCiuc001wwn.3. human. [Q96L50-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY052405 mRNA. Translation: AAL11430.1.
BX248298 mRNA. Translation: CAD62625.1. Different initiation.
AK293156 mRNA. Translation: BAG56701.1.
CH471078 Genomic DNA. Translation: EAW65761.1.
BC030142 mRNA. Translation: AAH30142.1.
BC093697 mRNA. Translation: AAH93697.1.
BC112241 mRNA. Translation: AAI12242.1.
BC139921 mRNA. Translation: AAI39922.1.
CCDSiCCDS9686.1. [Q96L50-1]
CCDS9687.1. [Q96L50-2]
RefSeqiNP_689542.2. NM_152329.3. [Q96L50-1]
NP_982292.1. NM_203467.1. [Q96L50-2]
UniGeneiHs.451090.

3D structure databases

ProteinModelPortaliQ96L50.
SMRiQ96L50. Positions 115-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125793. 26 interactions.
IntActiQ96L50. 15 interactions.
STRINGi9606.ENSP00000298288.

PTM databases

iPTMnetiQ96L50.
PhosphoSiteiQ96L50.

Polymorphism and mutation databases

BioMutaiLRR1.
DMDMi37079896.

Proteomic databases

EPDiQ96L50.
MaxQBiQ96L50.
PaxDbiQ96L50.
PRIDEiQ96L50.

Protocols and materials databases

DNASUi122769.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298288; ENSP00000298288; ENSG00000165501. [Q96L50-1]
ENST00000318317; ENSP00000315628; ENSG00000165501. [Q96L50-2]
GeneIDi122769.
KEGGihsa:122769.
UCSCiuc001wwn.3. human. [Q96L50-1]

Organism-specific databases

CTDi122769.
GeneCardsiLRR1.
H-InvDBHIX0037761.
HGNCiHGNC:19742. LRR1.
MIMi609193. gene.
neXtProtiNX_Q96L50.
PharmGKBiPA134915321.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00530000063533.
HOGENOMiHOG000273865.
HOVERGENiHBG045576.
InParanoidiQ96L50.
KOiK10348.
OMAiKTCVCGR.
OrthoDBiEOG7KQ229.
PhylomeDBiQ96L50.
TreeFamiTF319257.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GenomeRNAii122769.
NextBioi80991.
PROiQ96L50.
SOURCEiSearch...

Gene expression databases

BgeeiQ96L50.
CleanExiHS_PPIL5.
ExpressionAtlasiQ96L50. baseline and differential.
GenevisibleiQ96L50. HS.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF12799. LRR_4. 1 hit.
PF13516. LRR_6. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 4 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel leucine-rich repeat protein (LRR-1): potential involvement in 4-1BB-mediated signal transduction."
    Jang I.-K., Lee Z.-H., Kim H.-H., Hill J.M., Kim J.-D., Kwon B.S.
    Mol. Cells 12:304-312(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION.
    Tissue: T-cell lymphoma.
  2. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Cervix carcinoma.
  3. "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] (ISOFORM 1).
    Tissue: Neuroblastoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: B-cell, Heart and Lung.
  6. "VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases."
    Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C., Conaway J.W., Nakayama K.I.
    Genes Dev. 18:3055-3065(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AN E3 UBIQUITIN LIGASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CUL2; RBX1; TCEB1 AND TCEB2, MUTAGENESIS OF 341-HIS--PRO-344.

Entry informationi

Entry nameiLLR1_HUMAN
AccessioniPrimary (citable) accession number: Q96L50
Secondary accession number(s): A5D6X3
, B4DDE0, Q52M24, Q86SZ1, Q8N6H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: May 11, 2016
This is version 125 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.