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Protein

Ligand of Numb protein X 2

Gene

Lnx2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri51 – 8939RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • PDZ domain binding Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • protein homooligomerization Source: MGI
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Ligand of Numb protein X 2
Alternative name(s):
Numb-binding protein 2
Gene namesi
Name:Lnx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2155959. Lnx2.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi207 – 2104NPAF → I: Abolishes binding to NUMB protein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 687687Ligand of Numb protein X 2PRO_0000055916Add
BLAST

Proteomic databases

EPDiQ91XL2.
MaxQBiQ91XL2.
PaxDbiQ91XL2.
PRIDEiQ91XL2.

PTM databases

iPTMnetiQ91XL2.
PhosphoSiteiQ91XL2.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ91XL2.
CleanExiMM_LNX2.
GenevisibleiQ91XL2. MM.

Interactioni

Subunit structurei

Interacts with the phosphotyrosine interaction domain of NUMB.1 Publication

GO - Molecular functioni

  • PDZ domain binding Source: MGI

Protein-protein interaction databases

BioGridi228328. 3 interactions.
STRINGi10090.ENSMUSP00000016664.

Structurei

3D structure databases

ProteinModelPortaliQ91XL2.
SMRiQ91XL2. Positions 37-111, 228-680.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini232 – 31786PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini338 – 42184PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini465 – 55187PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini597 – 68589PDZ 4PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 2104NPXY motif

Domaini

The NPXY motif is required for the interaction with the PID domain of NUMB. It is however not sufficient.

Sequence similaritiesi

Contains 4 PDZ (DHR) domains.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri51 – 8939RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITAD. Eukaryota.
ENOG410Y9FS. LUCA.
GeneTreeiENSGT00760000119017.
HOGENOMiHOG000261605.
HOVERGENiHBG039539.
InParanoidiQ91XL2.
KOiK10692.
OMAiEKDFCPL.
OrthoDBiEOG75F4CJ.
TreeFamiTF330709.

Family and domain databases

Gene3Di2.30.42.10. 4 hits.
3.30.40.10. 1 hit.
InterProiIPR001478. PDZ.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00595. PDZ. 4 hits.
[Graphical view]
SMARTiSM00228. PDZ. 4 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 4 hits.
PROSITEiPS50106. PDZ. 4 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91XL2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTTSDEMVP VEQASSTSSL DPLCFECGQQ HWARENHLYN YQGEVDDDLV
60 70 80 90 100
CHICLQPLLQ PLDTPCGHTF CHKCLRNFLQ EKDFCPLDRK RLHFKLCKKS
110 120 130 140 150
SILVHKLLDK LLVLCPFSPV CQDVMQRCDL EAHLKNRCPG ASHRRVDLER
160 170 180 190 200
RKTSQTQTQI EGETGSTVID PPGTLPPETD CSGTVPGERN LTPASLPVWT
210 220 230 240 250
EEPGLDNPAF EESAAADSVQ QPLSLPEGEI TTIEIHRSNP YIQLGISIVG
260 270 280 290 300
GNETPLINIV IQEVYRDGVI ARDGRLLAGD QILQVNNYDI SNVSHNHARA
310 320 330 340 350
VLSQPCSTLQ LTVLRERRFG SRANSHADGS APRDEVFQVL LHKRDSTEQL
360 370 380 390 400
GIKLVRRTDE PGVFILDLLE GGLAAQDGRL NSNDRVLAIN GHDLKHGTPE
410 420 430 440 450
LAAQIIQASG ERVNLTIARP GKPQPSNGSR EAGAHSSSNH AQPPSHSRPG
460 470 480 490 500
SHKDLTRCVT CQEKHITVKK EPHESLGMTV AGGRGSKSGE LPIFVTSVPP
510 520 530 540 550
HGCLARDGRI KRGDVLLNIN GIDLTNLSHS EAVAMLKASA ASPAVILKAL
560 570 580 590 600
EVQIAEEAAQ ATEEQPSAFS ENEYDASWSP SWVMWLGLPS ALHSCHDIVL
610 620 630 640 650
RRSYLGSWGF SIVGGYEENH TNQPFFIKTI VLGTPAYYDG RLKCGDMIVA
660 670 680
VNGLSTVGMS HSALVPMLKE QRNKVTLTVI CWPGSLV
Length:687
Mass (Da):75,129
Last modified:July 27, 2011 - v2
Checksum:i5B21B2D929C295D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti648 – 6481I → M in AAK94476 (PubMed:11922143).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF401681 mRNA. Translation: AAK94476.1.
AK036218 mRNA. Translation: BAC29350.1.
AL513345 Genomic DNA. Translation: CAO77963.1.
CH466614 Genomic DNA. Translation: EDL05824.1.
CCDSiCCDS19875.1.
RefSeqiNP_542985.4. NM_080795.4.
XP_006504863.1. XM_006504800.2.
UniGeneiMm.272203.

Genome annotation databases

EnsembliENSMUST00000016664; ENSMUSP00000016664; ENSMUSG00000016520.
GeneIDi140887.
KEGGimmu:140887.
UCSCiuc009ant.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF401681 mRNA. Translation: AAK94476.1.
AK036218 mRNA. Translation: BAC29350.1.
AL513345 Genomic DNA. Translation: CAO77963.1.
CH466614 Genomic DNA. Translation: EDL05824.1.
CCDSiCCDS19875.1.
RefSeqiNP_542985.4. NM_080795.4.
XP_006504863.1. XM_006504800.2.
UniGeneiMm.272203.

3D structure databases

ProteinModelPortaliQ91XL2.
SMRiQ91XL2. Positions 37-111, 228-680.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228328. 3 interactions.
STRINGi10090.ENSMUSP00000016664.

PTM databases

iPTMnetiQ91XL2.
PhosphoSiteiQ91XL2.

Proteomic databases

EPDiQ91XL2.
MaxQBiQ91XL2.
PaxDbiQ91XL2.
PRIDEiQ91XL2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000016664; ENSMUSP00000016664; ENSMUSG00000016520.
GeneIDi140887.
KEGGimmu:140887.
UCSCiuc009ant.2. mouse.

Organism-specific databases

CTDi222484.
MGIiMGI:2155959. Lnx2.

Phylogenomic databases

eggNOGiENOG410ITAD. Eukaryota.
ENOG410Y9FS. LUCA.
GeneTreeiENSGT00760000119017.
HOGENOMiHOG000261605.
HOVERGENiHBG039539.
InParanoidiQ91XL2.
KOiK10692.
OMAiEKDFCPL.
OrthoDBiEOG75F4CJ.
TreeFamiTF330709.

Miscellaneous databases

ChiTaRSiLnx2. mouse.
NextBioi370025.
PROiQ91XL2.
SOURCEiSearch...

Gene expression databases

BgeeiQ91XL2.
CleanExiMM_LNX2.
GenevisibleiQ91XL2. MM.

Family and domain databases

Gene3Di2.30.42.10. 4 hits.
3.30.40.10. 1 hit.
InterProiIPR001478. PDZ.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00595. PDZ. 4 hits.
[Graphical view]
SMARTiSM00228. PDZ. 4 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 4 hits.
PROSITEiPS50106. PDZ. 4 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Lnx family proteins function as molecular scaffolds for Numb family proteins."
    Rice D.S., Northcutt G.M., Kurschner C.
    Mol. Cell. Neurosci. 18:525-540(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH NUMB, MUTAGENESIS OF 207-ASN--PHE-210.
    Strain: BALB/cJ.
    Tissue: Cerebellum.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiLNX2_MOUSE
AccessioniPrimary (citable) accession number: Q91XL2
Secondary accession number(s): A6PW04, Q8CBE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.