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O70263

- LNX1_MOUSE

UniProt

O70263 - LNX1_MOUSE

Protein

E3 ubiquitin-protein ligase LNX

Gene

Lnx1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65.
    Isoform 2 provides an endocytic scaffold for IGSF5/JAM4.

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri45 – 8339RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. PDZ domain binding Source: MGI
    3. protein binding Source: MGI
    4. ubiquitin-protein transferase activity Source: MGI
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. protein homooligomerization Source: MGI
    2. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: MGI
    3. ubiquitin-dependent protein catabolic process Source: MGI

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase LNX (EC:6.3.2.-)
    Alternative name(s):
    Ligand of Numb protein X 1
    Ligand of Numb-binding protein 1
    Numb-binding protein 1
    Gene namesi
    Name:Lnx1
    Synonyms:Lnx
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1278335. Lnx1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481C → A: Loss of function. 1 Publication
    Mutagenesisi181 – 1811P → A: No effect on binding to NUMB protein. 1 Publication
    Mutagenesisi182 – 1821G → A: Slightly affects binding to NUMB protein. 1 Publication
    Mutagenesisi183 – 1831L → A: Abolishes binding to NUMB protein. 1 Publication
    Mutagenesisi184 – 1841D → A: Slightly affects binding to NUMB protein. 1 Publication
    Mutagenesisi185 – 1851N → A: Abolishes binding to NUMB protein. 1 Publication
    Mutagenesisi186 – 1861P → A: Slightly affects binding to NUMB protein. 1 Publication
    Mutagenesisi188 – 1881Y → A: Abolishes binding to NUMB protein. 1 Publication
    Mutagenesisi188 – 1881Y → F: No effect on binding to NUMB protein. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 728728E3 ubiquitin-protein ligase LNXPRO_0000055914Add
    BLAST

    Proteomic databases

    PaxDbiO70263.
    PRIDEiO70263.

    PTM databases

    PhosphoSiteiO70263.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are expressed in the heart. Isoform 1 is also expressed in kidney, lung and skeletal muscle while isoform 2 is also expressed in brain.1 Publication

    Gene expression databases

    ArrayExpressiO70263.
    BgeeiO70263.
    CleanExiMM_LNX1.
    GenevestigatoriO70263.

    Interactioni

    Subunit structurei

    Interacts with CXADR. Interacts with MAGEB18 and MAGEF1 By similarity. Interacts with the phosphotyrosine interaction domain of all isoforms of NUMB. IGSF5/JAM4 interacts with isoform 2 through the second PDZ domain, other isoforms may also interact with IGSF5/JAM4.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi201187. 8 interactions.
    IntActiO70263. 3 interactions.
    MINTiMINT-253029.

    Structurei

    Secondary structure

    1
    728
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi384 – 3896
    Beta strandi398 – 4025
    Beta strandi405 – 4073
    Beta strandi409 – 4157
    Helixi420 – 4245
    Beta strandi432 – 4365
    Helixi446 – 45510
    Beta strandi456 – 46510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VQFX-ray1.20A381-467[»]
    3VQGX-ray1.35A381-467[»]
    ProteinModelPortaliO70263.
    SMRiO70263. Positions 45-130, 277-722.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini278 – 36285PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini385 – 46783PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini508 – 59386PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini638 – 72386PDZ 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni186 – 24459Interaction with MAGEB18By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi185 – 1884NPXY motif

    Domaini

    The NPXY motif is required for the interaction with the PID domain of NUMB. It is however not sufficient.
    The PDZ 1 domain participates in the interaction with the PID domain of NUMB, and participates in the isoform-specific ubiquitination of NUMB. The PDZ 2 domain of isoform 2 participates in the interaction with IGSF5/JAM4, other isoforms containing this domain may also interact with IGSF5/JAM4.

    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 fingeri45 – 8339RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG236845.
    GeneTreeiENSGT00740000115038.
    HOGENOMiHOG000261605.
    HOVERGENiHBG039539.
    InParanoidiO70263.
    KOiK10692.
    OMAiVFPRLYH.
    OrthoDBiEOG75F4CJ.
    PhylomeDBiO70263.
    TreeFamiTF330709.

    Family and domain databases

    Gene3Di2.30.42.10. 4 hits.
    3.30.40.10. 1 hit.
    InterProiIPR001478. PDZ.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00595. PDZ. 4 hits.
    PF00097. zf-C3HC4. 1 hit.
    [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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O70263-1) [UniParc]FASTAAdd to Basket

    Also known as: LNX, LNXp80

    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

    MNQPDLADDP DPSPEPLCIV CGQNHSPEEN HFYTYTEDVD DDLICHICLQ    50
    ALLDPLDTPC GHTYCTLCLT NFLVEKDFCP VDRKPVVLQH CKKSSILVNK 100
    LLNKLLVTCP FTEHCTEVLQ RCDLQHHFQT SCKGASHYGL TKDRKRRSQD 150
    GCPDGCASLM ATTLSPEVSA AATISLMTDE PGLDNPAYVS SVEDGEPVAN 200
    SSDSGRSNRT RARPFERSTM RSRSFKKINR ALSALRRTKS GSVVANHVDQ 250
    GRDNSENTTV PEVFPRLFHL IPDGEITSIK INRADPSESL SIRLVGGSET 300
    PLVHIIIQHI YRDGVIARDG RLLPGDIILK VNGMDISNVP HNYAVRLLRQ 350
    PCQVLRLTVL REQKFRSRSN AHVPDSYGPR DDSFHVILNK SSPEEQLGIK 400
    LVRRVDEPGV FIFNVLNGGV ADRHGQLEEN DRVLAINGHD LRFGSPESAA 450
    HLIQASERRV HLVVSRQVRQ SSPDIFQEAG WISNGQQSPG PGERNTASKP 500
    AATCHEKVVS VWKDPSESLG MTVGGGASHR EWDLPIYVIS VEPGGVISRD 550
    GRIKTGDILL NVNGIELTEV SRTEAVAILK SAPSSVVLKA LEVKEQEAQE 600
    DCSPAALDSN HNVTPPGDWS PSWVMWLELP QYLCNCKDVI LRRNTAGSLG 650
    FCIVGGYEEY SGNKPFFIKS IVEGTPAYND GRIRCGDILL AVNGRSTSGM 700
    IHACLARMLK ELKGRITLTI ASWPGTFL 728
    Length:728
    Mass (Da):80,157
    Last modified:August 1, 1998 - v1
    Checksum:iE2914BD364C0CEC4
    GO
    Isoform 2 (identifier: O70263-2) [UniParc]FASTAAdd to Basket

    Also known as: LNX-B, LNXp70

    The sequence of this isoform differs from the canonical sequence as follows:
         1-131: MNQPDLADDP...CDLQHHFQTS → MKALLLLVLPWLSPANYIDNVGNLHFLYSEL

    Show »
    Length:628
    Mass (Da):68,790
    Checksum:iF4CC529ED9D33D55
    GO
    Isoform 3 (identifier: O70263-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-131: MNQPDLADDP...CDLQHHFQTS → MKALLLLVLPWLSPANYIDNVGNLHFLYSEL
         332-357: NGMDISNVPHNYAVRLLRQPCQVLRL → PMRRELVTIGYKIVSCRLCVAHNLSP
         358-728: Missing.

    Note: No experimental conformation available.

    Show »
    Length:257
    Mass (Da):28,202
    Checksum:iADCE0552F3BAA28D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti258 – 2581T → N in BAC31789. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 131131MNQPD…HFQTS → MKALLLLVLPWLSPANYIDN VGNLHFLYSEL in isoform 2 and isoform 3. 3 PublicationsVSP_005734Add
    BLAST
    Alternative sequencei332 – 35726NGMDI…QVLRL → PMRRELVTIGYKIVSCRLCV AHNLSP in isoform 3. 1 PublicationVSP_012588Add
    BLAST
    Alternative sequencei358 – 728371Missing in isoform 3. 1 PublicationVSP_012589Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF034745 mRNA. Translation: AAC40075.1.
    AF034746 mRNA. Translation: AAC40076.1.
    AK044127 mRNA. Translation: BAC31789.1.
    BC040367 mRNA. Translation: AAH40367.1.
    CCDSiCCDS19347.1. [O70263-2]
    CCDS51524.1. [O70263-1]
    PIRiT09457.
    T09458.
    RefSeqiNP_001153049.1. NM_001159577.1. [O70263-1]
    NP_001153050.1. NM_001159578.1.
    NP_001153051.1. NM_001159579.1. [O70263-2]
    NP_001153052.1. NM_001159580.1.
    NP_034857.3. NM_010727.4. [O70263-2]
    XP_006504317.1. XM_006504254.1. [O70263-1]
    UniGeneiMm.440403.

    Genome annotation databases

    EnsembliENSMUST00000039744; ENSMUSP00000040098; ENSMUSG00000029228. [O70263-2]
    ENSMUST00000087161; ENSMUSP00000084405; ENSMUSG00000029228. [O70263-1]
    ENSMUST00000117388; ENSMUSP00000113035; ENSMUSG00000029228. [O70263-1]
    ENSMUST00000117525; ENSMUSP00000113837; ENSMUSG00000029228. [O70263-2]
    GeneIDi16924.
    KEGGimmu:16924.
    UCSCiuc008xtr.2. mouse. [O70263-1]
    uc008xtu.2. mouse. [O70263-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF034745 mRNA. Translation: AAC40075.1 .
    AF034746 mRNA. Translation: AAC40076.1 .
    AK044127 mRNA. Translation: BAC31789.1 .
    BC040367 mRNA. Translation: AAH40367.1 .
    CCDSi CCDS19347.1. [O70263-2 ]
    CCDS51524.1. [O70263-1 ]
    PIRi T09457.
    T09458.
    RefSeqi NP_001153049.1. NM_001159577.1. [O70263-1 ]
    NP_001153050.1. NM_001159578.1.
    NP_001153051.1. NM_001159579.1. [O70263-2 ]
    NP_001153052.1. NM_001159580.1.
    NP_034857.3. NM_010727.4. [O70263-2 ]
    XP_006504317.1. XM_006504254.1. [O70263-1 ]
    UniGenei Mm.440403.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VQF X-ray 1.20 A 381-467 [» ]
    3VQG X-ray 1.35 A 381-467 [» ]
    ProteinModelPortali O70263.
    SMRi O70263. Positions 45-130, 277-722.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201187. 8 interactions.
    IntActi O70263. 3 interactions.
    MINTi MINT-253029.

    PTM databases

    PhosphoSitei O70263.

    Proteomic databases

    PaxDbi O70263.
    PRIDEi O70263.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000039744 ; ENSMUSP00000040098 ; ENSMUSG00000029228 . [O70263-2 ]
    ENSMUST00000087161 ; ENSMUSP00000084405 ; ENSMUSG00000029228 . [O70263-1 ]
    ENSMUST00000117388 ; ENSMUSP00000113035 ; ENSMUSG00000029228 . [O70263-1 ]
    ENSMUST00000117525 ; ENSMUSP00000113837 ; ENSMUSG00000029228 . [O70263-2 ]
    GeneIDi 16924.
    KEGGi mmu:16924.
    UCSCi uc008xtr.2. mouse. [O70263-1 ]
    uc008xtu.2. mouse. [O70263-3 ]

    Organism-specific databases

    CTDi 84708.
    MGIi MGI:1278335. Lnx1.

    Phylogenomic databases

    eggNOGi NOG236845.
    GeneTreei ENSGT00740000115038.
    HOGENOMi HOG000261605.
    HOVERGENi HBG039539.
    InParanoidi O70263.
    KOi K10692.
    OMAi VFPRLYH.
    OrthoDBi EOG75F4CJ.
    PhylomeDBi O70263.
    TreeFami TF330709.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi LNX1. mouse.
    NextBioi 290980.
    PROi O70263.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O70263.
    Bgeei O70263.
    CleanExi MM_LNX1.
    Genevestigatori O70263.

    Family and domain databases

    Gene3Di 2.30.42.10. 4 hits.
    3.30.40.10. 1 hit.
    InterProi IPR001478. PDZ.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00595. PDZ. 4 hits.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00228. PDZ. 4 hits.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 4 hits.
    PROSITEi PS50106. PDZ. 4 hits.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The mammalian numb phosphotyrosine-binding domain. Characterization of binding specificity and identification of a novel PDZ domain-containing numb binding protein, LNX."
      Dho S.E., Jacob S., Wolting C.D., French M.B., Rohrschneider L.R., McGlade C.J.
      J. Biol. Chem. 273:9179-9187(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-181; GLY-182; LEU-183; ASP-184; ASN-185; PRO-186 AND TYR-188.
      Tissue: Brain and Embryo.
    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] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Brain cortex.
    3. "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 3).
      Tissue: Eye.
    4. "LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation."
      Nie J., McGill M.A., Dermer M., Dho S.E., Wolting C.D., McGlade C.J.
      EMBO J. 21:93-102(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN NPXY MOTIF, MUTAGENESIS OF CYS-48.
    5. "A novel PTB-PDZ domain interaction mediates isoform-specific ubiquitylation of mammalian Numb."
      Nie J., Li S.S.-C., McGlade C.J.
      J. Biol. Chem. 279:20807-20815(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAINS PDZ, INTERACTION WITH NUMB.
    6. "Ligand-of-Numb protein X is an endocytic scaffold for junctional adhesion molecule 4."
      Kansaku A., Hirabayashi S., Mori H., Fujiwara N., Kawata A., Ikeda M., Rokukawa C., Kurihara H., Hata Y.
      Oncogene 25:5071-5084(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IGSF5.

    Entry informationi

    Entry nameiLNX1_MOUSE
    AccessioniPrimary (citable) accession number: O70263
    Secondary accession number(s): O70264, Q8BRI8, Q8CFR3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3