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Q9HBW1

- LRRC4_HUMAN

UniProt

Q9HBW1 - LRRC4_HUMAN

Protein

Leucine-rich repeat-containing protein 4

Gene

LRRC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (01 Oct 2001)
      Previous versions | rss
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    Functioni

    Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitment of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays a important role for auditory synaptic responses. Involved in the suppression of glioma By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct

    Protein family/group databases

    MEROPSiI43.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leucine-rich repeat-containing protein 4
    Alternative name(s):
    Brain tumor-associated protein BAG
    Nasopharyngeal carcinoma-associated gene 14 protein
    Netrin-G2 ligand
    Short name:
    NGL-2
    Gene namesi
    Name:LRRC4
    Synonyms:BAG
    ORF Names:NAG14, UNQ554/PRO1111
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:15586. LRRC4.

    Subcellular locationi

    Membrane; Single-pass type I membrane protein. Cell junctionsynapsepostsynaptic cell membrane By similarity
    Note: LRRC4 and DLG4 are interdependent for synaptic localization.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. integral component of membrane Source: UniProtKB-KW
    3. postsynaptic membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30463.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838Sequence AnalysisAdd
    BLAST
    Chaini39 – 653615Leucine-rich repeat-containing protein 4PRO_0000014833Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 521 PublicationPROSITE-ProRule annotation
    Disulfide bondi50 ↔ 611 PublicationPROSITE-ProRule annotation
    Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi304 ↔ 3291 PublicationPROSITE-ProRule annotation
    Disulfide bondi306 ↔ 3501 PublicationPROSITE-ProRule annotation
    Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi374 ↔ 4241 PublicationPROSITE-ProRule annotation
    Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi434 – 4341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9HBW1.
    PRIDEiQ9HBW1.

    PTM databases

    PhosphoSiteiQ9HBW1.

    Expressioni

    Tissue specificityi

    Specifically expressed in brain.1 Publication

    Gene expression databases

    ArrayExpressiQ9HBW1.
    BgeeiQ9HBW1.
    CleanExiHS_LRRC4.
    GenevestigatoriQ9HBW1.

    Organism-specific databases

    HPAiHPA051100.

    Interactioni

    Subunit structurei

    Interacts with DLG4 By similarity. Interacts (via LRR repeats) with NTNG2. Forms a complex with DLG4 and with NMDA receptors.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NTNG1Q9Y2I22EBI-7444327,EBI-7444396
    NTNG2Q96CW94EBI-7444327,EBI-750795

    Protein-protein interaction databases

    BioGridi122061. 1 interaction.
    IntActiQ9HBW1. 3 interactions.
    MINTiMINT-6489320.
    STRINGi9606.ENSP00000249363.

    Structurei

    Secondary structure

    1
    653
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 523
    Beta strandi54 – 563
    Beta strandi58 – 603
    Beta strandi78 – 814
    Turni92 – 976
    Beta strandi103 – 1053
    Turni116 – 1216
    Beta strandi127 – 1293
    Turni140 – 1423
    Beta strandi143 – 1453
    Beta strandi151 – 1533
    Turni164 – 1696
    Beta strandi175 – 1773
    Turni189 – 1946
    Beta strandi200 – 2023
    Beta strandi222 – 2243
    Beta strandi231 – 2333
    Helixi235 – 2384
    Beta strandi246 – 2483
    Turni259 – 2646
    Beta strandi270 – 2723
    Beta strandi294 – 2963
    Turni306 – 3083
    Helixi309 – 31810
    Beta strandi328 – 3325
    Turni333 – 3375
    Helixi345 – 3473
    Beta strandi362 – 3654
    Beta strandi370 – 3723
    Beta strandi380 – 3856
    Turni387 – 3893
    Beta strandi390 – 3934
    Beta strandi399 – 4035
    Beta strandi405 – 4073
    Beta strandi409 – 4135
    Turni416 – 4183
    Beta strandi420 – 4278
    Beta strandi432 – 4409

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DL9NMR-A353-442[»]
    3ZYIX-ray2.60A1-444[»]
    ProteinModelPortaliQ9HBW1.
    SMRiQ9HBW1. Positions 44-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HBW1.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini39 – 527489ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini549 – 653105CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei528 – 54821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 7537LRRNTAdd
    BLAST
    Repeati76 – 9722LRR 1Add
    BLAST
    Repeati100 – 12122LRR 2Add
    BLAST
    Repeati124 – 14522LRR 3Add
    BLAST
    Repeati148 – 16922LRR 4Add
    BLAST
    Repeati172 – 19423LRR 5Add
    BLAST
    Repeati197 – 21822LRR 6Add
    BLAST
    Repeati219 – 24022LRR 7Add
    BLAST
    Repeati243 – 26422LRR 8Add
    BLAST
    Repeati267 – 28822LRR 9Add
    BLAST
    Domaini300 – 35253LRRCTAdd
    BLAST
    Domaini353 – 44290Ig-likeAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi455 – 52672Thr-richAdd
    BLAST

    Domaini

    The last 4 C-terminal residues bind to the first 2 PDZ domains of DLG4.By similarity

    Sequence similaritiesi

    Contains 9 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 LRRNT domain.Curated

    Keywords - Domaini

    Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG4886.
    HOGENOMiHOG000252924.
    HOVERGENiHBG052359.
    InParanoidiQ9HBW1.
    KOiK16351.
    OMAiCGCEAVW.
    OrthoDBiEOG769ZHZ.
    PhylomeDBiQ9HBW1.
    TreeFamiTF324303.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR026906. LRR_5.
    IPR026882. Lrrc4.
    [Graphical view]
    PANTHERiPTHR24369:SF9. PTHR24369:SF9. 1 hit.
    PfamiPF07679. I-set. 1 hit.
    PF13306. LRR_5. 1 hit.
    PF13855. LRR_8. 1 hit.
    [Graphical view]
    SMARTiSM00408. IGc2. 1 hit.
    SM00369. LRR_TYP. 3 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS51450. LRR. 7 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9HBW1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLLWQVTVH HHTWNAILLP FVYLTAQVWI LCAAIAAAAS AGPQNCPSVC    50
    SCSNQFSKVV CTRRGLSEVP QGIPSNTRYL NLMENNIQMI QADTFRHLHH 100
    LEVLQLGRNS IRQIEVGAFN GLASLNTLEL FDNWLTVIPS GAFEYLSKLR 150
    ELWLRNNPIE SIPSYAFNRV PSLMRLDLGE LKKLEYISEG AFEGLFNLKY 200
    LNLGMCNIKD MPNLTPLVGL EELEMSGNHF PEIRPGSFHG LSSLKKLWVM 250
    NSQVSLIERN AFDGLASLVE LNLAHNNLSS LPHDLFTPLR YLVELHLHHN 300
    PWNCDCDILW LAWWLREYIP TNSTCCGRCH APMHMRGRYL VEVDQASFQC 350
    SAPFIMDAPR DLNISEGRMA ELKCRTPPMS SVKWLLPNGT VLSHASRHPR 400
    ISVLNDGTLN FSHVLLSDTG VYTCMVTNVA GNSNASAYLN VSTAELNTSN 450
    YSFFTTVTVE TTEISPEDTT RKYKPVPTTS TGYQPAYTTS TTVLIQTTRV 500
    PKQVAVPATD TTDKMQTSLD EVMKTTKIII GCFVAVTLLA AAMLIVFYKL 550
    RKRHQQRSTV TAARTVEIIQ VDEDIPAATS AAATAAPSGV SGEGAVVLPT 600
    IHDHINYNTY KPAHGAHWTE NSLGNSLHPT VTTISEPYII QTHTKDKVQE 650
    TQI 653
    Length:653
    Mass (Da):72,717
    Last modified:October 1, 2001 - v2
    Checksum:i38159C81F6850E37
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41L → S in BAD18737. (PubMed:14702039)Curated
    Sequence conflicti253 – 2575QVSLI → H in CAC82651. 1 PublicationCurated
    Sequence conflicti300 – 3001N → D in BAD18737. (PubMed:14702039)Curated
    Sequence conflicti315 – 3151L → F in BAD18737. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti579 – 5791T → A in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035519

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF196976 mRNA. Translation: AAG28019.2.
    AJ297858 mRNA. Translation: CAC82651.1.
    AY358307 mRNA. Translation: AAQ88674.1.
    AK172751 mRNA. Translation: BAD18737.1.
    AK314047 mRNA. Translation: BAG36756.1.
    CH236947 Genomic DNA. Translation: EAL24316.1.
    BC111561 mRNA. Translation: AAI11562.1.
    BC111745 mRNA. Translation: AAI11746.1.
    CCDSiCCDS5799.1.
    RefSeqiNP_071426.1. NM_022143.4.
    UniGeneiHs.655003.

    Genome annotation databases

    EnsembliENST00000249363; ENSP00000249363; ENSG00000128594.
    GeneIDi64101.
    KEGGihsa:64101.
    UCSCiuc003vmk.3. human.

    Polymorphism databases

    DMDMi51701696.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF196976 mRNA. Translation: AAG28019.2 .
    AJ297858 mRNA. Translation: CAC82651.1 .
    AY358307 mRNA. Translation: AAQ88674.1 .
    AK172751 mRNA. Translation: BAD18737.1 .
    AK314047 mRNA. Translation: BAG36756.1 .
    CH236947 Genomic DNA. Translation: EAL24316.1 .
    BC111561 mRNA. Translation: AAI11562.1 .
    BC111745 mRNA. Translation: AAI11746.1 .
    CCDSi CCDS5799.1.
    RefSeqi NP_071426.1. NM_022143.4.
    UniGenei Hs.655003.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DL9 NMR - A 353-442 [» ]
    3ZYI X-ray 2.60 A 1-444 [» ]
    ProteinModelPortali Q9HBW1.
    SMRi Q9HBW1. Positions 44-441.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122061. 1 interaction.
    IntActi Q9HBW1. 3 interactions.
    MINTi MINT-6489320.
    STRINGi 9606.ENSP00000249363.

    Protein family/group databases

    MEROPSi I43.001.

    PTM databases

    PhosphoSitei Q9HBW1.

    Polymorphism databases

    DMDMi 51701696.

    Proteomic databases

    PaxDbi Q9HBW1.
    PRIDEi Q9HBW1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000249363 ; ENSP00000249363 ; ENSG00000128594 .
    GeneIDi 64101.
    KEGGi hsa:64101.
    UCSCi uc003vmk.3. human.

    Organism-specific databases

    CTDi 64101.
    GeneCardsi GC07M127667.
    HGNCi HGNC:15586. LRRC4.
    HPAi HPA051100.
    MIMi 610486. gene.
    neXtProti NX_Q9HBW1.
    PharmGKBi PA30463.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000252924.
    HOVERGENi HBG052359.
    InParanoidi Q9HBW1.
    KOi K16351.
    OMAi CGCEAVW.
    OrthoDBi EOG769ZHZ.
    PhylomeDBi Q9HBW1.
    TreeFami TF324303.

    Miscellaneous databases

    EvolutionaryTracei Q9HBW1.
    GeneWikii LRRC4.
    GenomeRNAii 64101.
    NextBioi 65940.
    PROi Q9HBW1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HBW1.
    Bgeei Q9HBW1.
    CleanExi HS_LRRC4.
    Genevestigatori Q9HBW1.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR000483. Cys-rich_flank_reg_C.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR026906. LRR_5.
    IPR026882. Lrrc4.
    [Graphical view ]
    PANTHERi PTHR24369:SF9. PTHR24369:SF9. 1 hit.
    Pfami PF07679. I-set. 1 hit.
    PF13306. LRR_5. 1 hit.
    PF13855. LRR_8. 1 hit.
    [Graphical view ]
    SMARTi SM00408. IGc2. 1 hit.
    SM00369. LRR_TYP. 3 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS51450. LRR. 7 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression and functional characterization of LRRC4, a novel brain-specific member of the LRR superfamily."
      Zhang Q., Wang J., Fan S., Wang L., Cao L., Tang K., Peng C., Li Z., Li W., Gan K., Liu Z., Li X., Shen S., Li G.
      FEBS Lett. 579:3674-3682(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. Wang J.
      Thesis (2000), Zhongshan Medical University / Guangzhou, China
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
    7. "Solution structure of the Ig-like domain of human leucine-rich repeat-containing protein 4."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 351-442.
    8. "Structural basis for cell surface patterning through NetrinG-NGL interactions."
      Seiradake E., Coles C.H., Perestenko P.V., Harlos K., McIlhinney R.A., Aricescu A.R., Jones E.Y.
      EMBO J. 30:4479-4488(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-444 IN COMPLEX WITH NTNG2, DISULFIDE BONDS.
    9. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-579.

    Entry informationi

    Entry nameiLRRC4_HUMAN
    AccessioniPrimary (citable) accession number: Q9HBW1
    Secondary accession number(s): A4D0Y9
    , Q14DU9, Q6ZMI8, Q96A85
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 122 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 7
      Human chromosome 7: 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

    Dasty 3