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Q9HBW1

- LRRC4_HUMAN

UniProt

Q9HBW1 - LRRC4_HUMAN

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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

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 - Biological processi

  1. postsynaptic density protein 95 clustering Source: Ensembl
  2. regulation of synapse organization Source: Ensembl
  3. synapse organization Source: Ensembl
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini39 – 527489ExtracellularSequence AnalysisAdd
BLAST
Transmembranei528 – 54821HelicalSequence AnalysisAdd
BLAST
Topological domaini549 – 653105CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. dendritic spine Source: Ensembl
  3. excitatory synapse Source: Ensembl
  4. integral component of membrane Source: UniProtKB-KW
  5. postsynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiQ9HBW1.
CleanExiHS_LRRC4.
ExpressionAtlasiQ9HBW1. baseline and differential.
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 – 523Combined sources
Beta strandi54 – 563Combined sources
Beta strandi58 – 603Combined sources
Beta strandi78 – 814Combined sources
Turni92 – 976Combined sources
Beta strandi103 – 1053Combined sources
Turni116 – 1216Combined sources
Beta strandi127 – 1293Combined sources
Turni140 – 1423Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi151 – 1533Combined sources
Turni164 – 1696Combined sources
Beta strandi175 – 1773Combined sources
Turni189 – 1946Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi222 – 2243Combined sources
Beta strandi231 – 2333Combined sources
Helixi235 – 2384Combined sources
Beta strandi246 – 2483Combined sources
Turni259 – 2646Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi294 – 2963Combined sources
Turni306 – 3083Combined sources
Helixi309 – 31810Combined sources
Beta strandi328 – 3325Combined sources
Turni333 – 3375Combined sources
Helixi345 – 3473Combined sources
Beta strandi362 – 3654Combined sources
Beta strandi370 – 3723Combined sources
Beta strandi380 – 3856Combined sources
Turni387 – 3893Combined sources
Beta strandi390 – 3934Combined sources
Beta strandi399 – 4035Combined sources
Beta strandi405 – 4073Combined sources
Beta strandi409 – 4135Combined sources
Turni416 – 4183Combined sources
Beta strandi420 – 4278Combined sources
Beta strandi432 – 4409Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9HBW1.

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.
GeneTreeiENSGT00760000118831.
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

        10         20         30         40         50
MKLLWQVTVH HHTWNAILLP FVYLTAQVWI LCAAIAAAAS AGPQNCPSVC
60 70 80 90 100
SCSNQFSKVV CTRRGLSEVP QGIPSNTRYL NLMENNIQMI QADTFRHLHH
110 120 130 140 150
LEVLQLGRNS IRQIEVGAFN GLASLNTLEL FDNWLTVIPS GAFEYLSKLR
160 170 180 190 200
ELWLRNNPIE SIPSYAFNRV PSLMRLDLGE LKKLEYISEG AFEGLFNLKY
210 220 230 240 250
LNLGMCNIKD MPNLTPLVGL EELEMSGNHF PEIRPGSFHG LSSLKKLWVM
260 270 280 290 300
NSQVSLIERN AFDGLASLVE LNLAHNNLSS LPHDLFTPLR YLVELHLHHN
310 320 330 340 350
PWNCDCDILW LAWWLREYIP TNSTCCGRCH APMHMRGRYL VEVDQASFQC
360 370 380 390 400
SAPFIMDAPR DLNISEGRMA ELKCRTPPMS SVKWLLPNGT VLSHASRHPR
410 420 430 440 450
ISVLNDGTLN FSHVLLSDTG VYTCMVTNVA GNSNASAYLN VSTAELNTSN
460 470 480 490 500
YSFFTTVTVE TTEISPEDTT RKYKPVPTTS TGYQPAYTTS TTVLIQTTRV
510 520 530 540 550
PKQVAVPATD TTDKMQTSLD EVMKTTKIII GCFVAVTLLA AAMLIVFYKL
560 570 580 590 600
RKRHQQRSTV TAARTVEIIQ VDEDIPAATS AAATAAPSGV SGEGAVVLPT
610 620 630 640 650
IHDHINYNTY KPAHGAHWTE NSLGNSLHPT VTTISEPYII QTHTKDKVQE

TQI
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00760000118831.
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

Bgeei Q9HBW1.
CleanExi HS_LRRC4.
ExpressionAtlasi Q9HBW1. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 124 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