Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y2I1

- NISCH_HUMAN

UniProt

Q9Y2I1 - NISCH_HUMAN

Protein

Nischarin

Gene

NISCH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Acts either as the functional imidazoline-1 receptor (I1R) candidate or as a membrane-associated mediator of the I1R signaling. Binds numerous imidazoline ligands that induces initiation of cell-signaling cascades triggering to cell survival, growth and migration. Its activation by the agonist rilmenidine induces an increase in phosphorylation of mitogen-activated protein kinases MAPK1 and MAPK3 in rostral ventrolateral medulla (RVLM) neurons that exhibited rilmenidine-evoked hypotension By similarity. Blocking its activation with efaroxan abolished rilmenidine-induced mitogen-activated protein kinase phosphorylation in RVLM neurons By similarity. Acts as a modulator of Rac-regulated signal transduction pathways By similarity. Suppresses Rac1-stimulated cell migration by interacting with PAK1 and inhibiting its kinase activity By similarity. Also blocks Pak-independent Rac signaling by interacting with RAC1 and inhibiting Rac1-stimulated NF-kB response element and cyclin D1 promoter activation By similarity. Inhibits also LIMK1 kinase activity by reducing LIMK1 'Tyr-508' phosphorylation By similarity. Inhibits Rac-induced cell migration and invasion in breast and colon epithelial cells By similarity. Inhibits lamellipodia formation, when overexpressed By similarity. Plays a role in protection against apoptosis. Involved in association with IRS4 in the enhancement of insulin activation of MAPK1 and MAPK3. When overexpressed, induces a redistribution of cell surface ITGA5 integrin to intracellular endosomal structures.By similarity5 Publications

    GO - Molecular functioni

    1. G-protein coupled amine receptor activity Source: Ensembl
    2. identical protein binding Source: IntAct
    3. phosphatidylinositol binding Source: InterPro
    4. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. apoptotic process Source: UniProtKB-KW
    3. glucose metabolic process Source: Ensembl
    4. negative regulation of cell migration Source: Ensembl
    5. norepinephrine secretion Source: Ensembl
    6. Rac protein signal transduction Source: Ensembl
    7. regulation of blood pressure Source: Ensembl
    8. regulation of synaptic transmission, GABAergic Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    SignaLinkiQ9Y2I1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nischarin
    Alternative name(s):
    Imidazoline receptor 1
    Short name:
    I-1
    Short name:
    IR1
    Imidazoline receptor antisera-selected protein
    Short name:
    hIRAS
    Imidazoline-1 receptor
    Short name:
    I1R
    Imidazoline-1 receptor candidate protein
    Short name:
    I-1 receptor candidate protein
    Short name:
    I1R candidate protein
    Gene namesi
    Name:NISCH
    Synonyms:IRAS, KIAA0975
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:18006. NISCH.

    Subcellular locationi

    Cell membrane. Cytoplasm. Early endosome. Recycling endosome
    Note: Enriched in the early/sorting and recycling endosomes. Colocalized in early/sorting endosomes with EEA1 and SNX2 and in recycling endosomes with transferrin receptor. Detected in the perinuclear region partially associated with punctate structures By similarity. Colocalizes with PAK1 in cytoplasm, vesicular structures in the perinuclear area and membrane ruffles By similarity. Colocalizes with RAC1 in the cytoplasm and vesicles structures By similarity. Colocalized with MAPK1 and MAPK3 in RVLM neurons By similarity.By similarity

    GO - Cellular componenti

    1. cytosol Source: BHF-UCL
    2. early endosome Source: UniProtKB-SubCell
    3. membrane Source: UniProtKB
    4. plasma membrane Source: BHF-UCL
    5. recycling endosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi49 – 491R → A: Inhibits targeting to endosomes. 1 Publication
    Mutagenesisi50 – 501Y → A: Inhibits targeting to endosomes. 1 Publication

    Organism-specific databases

    PharmGKBiPA31635.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 15041503NischarinPRO_0000348265Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei541 – 5411PhosphoserineBy similarity
    Modified residuei1284 – 12841Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2I1.
    PaxDbiQ9Y2I1.
    PRIDEiQ9Y2I1.

    PTM databases

    PhosphoSiteiQ9Y2I1.

    Expressioni

    Tissue specificityi

    Isoform 1, isoform 3 and isoform 4 are expressed in brain. Isoform 1 is expressed in endocrine tissues.2 Publications

    Gene expression databases

    ArrayExpressiQ9Y2I1.
    BgeeiQ9Y2I1.
    CleanExiHS_NISCH.
    GenevestigatoriQ9Y2I1.

    Organism-specific databases

    HPAiHPA023189.

    Interactioni

    Subunit structurei

    Homooligomer. Interacts with GRB2. Interacts with PIK3R1; probably associates with the PI3-kinase complex. Interacts with IRS4. Found in a complex with ITGA5 and PAK1. Found in a complex with LIMK1 and PAK1. Interacts with ITGA5 (via cytoplasmic domain); this interaction is direct. Interacts with PAK1 (via kinase domain); this interaction is direct and is increased upon activation of PAK1 By similarity. Interacts with LIMK1 (via PDZ and kinase domain); this interaction is direct By similarity. Interacts with LIMK2; this interaction depends on LIMK2 activity By similarity. Interacts with RAC1 (activated state) By similarity. Interacts with STK11; this interaction may increase STK11 activity.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-2688731,EBI-2688731
    Rab14P611079EBI-2688731,EBI-917845From a different organism.
    Rab4aP057144EBI-2688731,EBI-9029299From a different organism.
    RAB9AP511515EBI-2688731,EBI-4401353

    Protein-protein interaction databases

    BioGridi116358. 7 interactions.
    IntActiQ9Y2I1. 13 interactions.
    STRINGi9606.ENSP00000339958.

    Structurei

    Secondary structure

    1
    1504
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 258
    Beta strandi27 – 304
    Beta strandi32 – 387
    Beta strandi43 – 497
    Helixi50 – 6213
    Helixi85 – 10117
    Beta strandi105 – 1073
    Helixi109 – 1168

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3P0CX-ray2.27A/B18-124[»]
    ProteinModelPortaliQ9Y2I1.
    SMRiQ9Y2I1. Positions 18-123, 212-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 121111PXPROSITE-ProRule annotationAdd
    BLAST
    Repeati288 – 30922LRR 1Add
    BLAST
    Repeati311 – 33222LRR 2Add
    BLAST
    Repeati333 – 35422LRR 3Add
    BLAST
    Repeati356 – 37722LRR 4Add
    BLAST
    Repeati378 – 39922LRR 5Add
    BLAST
    Repeati403 – 42422LRR 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 133132Necessary for binding to phosphoinositide-3-P; not sufficient for targeting to endosomesAdd
    BLAST
    Regioni120 – 695576Necessary for homooligomerization and targeting to endosomesAdd
    BLAST
    Regioni245 – 869625Interaction with PAK1By similarityAdd
    BLAST
    Regioni660 – 869210Interaction with LIMKBy similarityAdd
    BLAST
    Regioni709 – 80799Interaction with ITGA5By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili634 – 69562Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi629 – 69163Glu-richAdd
    BLAST
    Compositional biasi1048 – 110457Ala/Pro-richAdd
    BLAST

    Domaini

    Both the presence of the PX domain and the coiled coil region are necessary for its endosomal targeting.

    Sequence similaritiesi

    Contains 6 LRR (leucine-rich) repeats.Curated
    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG269110.
    HOVERGENiHBG108189.
    InParanoidiQ9Y2I1.
    OMAiGNIEWAS.
    OrthoDBiEOG70ZZMH.
    PhylomeDBiQ9Y2I1.
    TreeFamiTF320547.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR001611. Leu-rich_rpt.
    IPR001683. Phox.
    [Graphical view]
    PfamiPF13855. LRR_8. 1 hit.
    PF00787. PX. 1 hit.
    [Graphical view]
    SMARTiSM00312. PX. 1 hit.
    [Graphical view]
    SUPFAMiSSF64268. SSF64268. 1 hit.
    PROSITEiPS51450. LRR. 6 hits.
    PS50195. PX. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y2I1-1) [UniParc]FASTAAdd to Basket

    Also known as: IRAS-1, IRAS-M

    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

    MATARTFGPE REAEPAKEAR VVGSELVDTY TVYIIQVTDG SHEWTVKHRY     50
    SDFHDLHEKL VAERKIDKNL LPPKKIIGKN SRSLVEKREK DLEVYLQKLL 100
    AAFPGVTPRV LAHFLHFHFY EINGITAALA EELFEKGEQL LGAGEVFAIG 150
    PLQLYAVTEQ LQQGKPTCAS GDAKTDLGHI LDFTCRLKYL KVSGTEGPFG 200
    TSNIQEQLLP FDLSIFKSLH QVEISHCDAK HIRGLVASKP TLATLSVRFS 250
    ATSMKEVLVP EASEFDEWEP EGTTLEGPVT AVIPTWQALT TLDLSHNSVS 300
    EIDESVKLIP KIEFLDLSHN GLLVVDNLQH LYNLVHLDLS YNKLSSLEGL 350
    HTKLGNIKTL NLAGNLLESL SGLHKLYSLV NLDLRDNRIE QMEEVRSIGS 400
    LPCLEHVSLL NNPLSIIPDY RTKVLAQFGE RASEVCLDDT VTTEKELDTV 450
    EVLKAIQKAK EVKSKLSNPE KKGGEDSRLS AAPCIRPSSS PPTVAPASAS 500
    LPQPILSNQG IMFVQEEALA SSLSSTDSLT PEHQPIAQGC SDSLESIPAG 550
    QAASDDLRDV PGAVGGASPE HAEPEVQVVP GSGQIIFLPF TCIGYTATNQ 600
    DFIQRLSTLI RQAIERQLPA WIEAANQREE GQGEQGEEED EEEEEEEDVA 650
    ENRYFEMGPP DVEEEEGGGQ GEEEEEEEED EEAEEERLAL EWALGADEDF 700
    LLEHIRILKV LWCFLIHVQG SIRQFAACLV LTDFGIAVFE IPHQESRGSS 750
    QHILSSLRFV FCFPHGDLTE FGFLMPELCL VLKVRHSENT LFIISDAANL 800
    HEFHADLRSC FAPQHMAMLC SPILYGSHTS LQEFLRQLLT FYKVAGGCQE 850
    RSQGCFPVYL VYSDKRMVQT AAGDYSGNIE WASCTLCSAV RRSCCAPSEA 900
    VKSAAIPYWL LLTPQHLNVI KADFNPMPNR GTHNCRNRNS FKLSRVPLST 950
    VLLDPTRSCT QPRGAFADGH VLELLVGYRF VTAIFVLPHE KFHFLRVYNQ 1000
    LRASLQDLKT VVIAKTPGTG GSPQGSFADG QPAERRASND QRPQEVPAEA 1050
    LAPAPAEVPA PAPAAASASG PAKTPAPAEA STSALVPEET PVEAPAPPPA 1100
    EAPAQYPSEH LIQATSEENQ IPSHLPACPS LRHVASLRGS AIIELFHSSI 1150
    AEVENEELRH LMWSSVVFYQ TPGLEVTACV LLSTKAVYFV LHDGLRRYFS 1200
    EPLQDFWHQK NTDYNNSPFH ISQCFVLKLS DLQSVNVGLF DQHFRLTGST 1250
    PMQVVTCLTR DSYLTHCFLQ HLMVVLSSLE RTPSPEPVDK DFYSEFGNKT 1300
    TGKMENYELI HSSRVKFTYP SEEEIGDLTF TVAQKMAEPE KAPALSILLY 1350
    VQAFQVGMPP PGCCRGPLRP KTLLLTSSEI FLLDEDCVHY PLPEFAKEPP 1400
    QRDRYRLDDG RRVRDLDRVL MGYQTYPQAL TLVFDDVQGH DLMGSVTLDH 1450
    FGEVPGGPAR ASQGREVQWQ VFVPSAESRE KLISLLARQW EALCGRELPV 1500
    ELTG 1504
    Length:1,504
    Mass (Da):166,629
    Last modified:May 18, 2010 - v3
    Checksum:i7761C7DA1FDC4E53
    GO
    Isoform 2 (identifier: Q9Y2I1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-511: Missing.

    Show »
    Length:993
    Mass (Da):110,194
    Checksum:iE0415818937AA523
    GO
    Isoform 3 (identifier: Q9Y2I1-3) [UniParc]FASTAAdd to Basket

    Also known as: IRAS-L

    The sequence of this isoform differs from the canonical sequence as follows:
         511-583: IMFVQEEALA...PEVQVVPGSG → NRVCTLLLVE...CLLGEDSQLL
         584-1504: Missing.

    Show »
    Length:583
    Mass (Da):63,997
    Checksum:i83CED19440961191
    GO
    Isoform 4 (identifier: Q9Y2I1-4) [UniParc]FASTAAdd to Basket

    Also known as: IRAS-S

    The sequence of this isoform differs from the canonical sequence as follows:
         512-515: MFVQ → LGDE
         516-1504: Missing.

    Show »
    Length:515
    Mass (Da):56,867
    Checksum:iB623BE4D42BBA51C
    GO

    Sequence cautioni

    The sequence BAA76819.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti927 – 9271M → I in AAH56900. (PubMed:15489334)Curated
    Sequence conflicti1023 – 10231P → A in BAA76819. (PubMed:10231032)Curated
    Sequence conflicti1123 – 11231S → P in AAH38102. (PubMed:15489334)Curated
    Sequence conflicti1382 – 13821L → F in AAH54494. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti299 – 2991V → I.6 Publications
    Corresponds to variant rs9856575 [ dbSNP | Ensembl ].
    VAR_046130
    Natural varianti1056 – 10561A → V.7 Publications
    Corresponds to variant rs887515 [ dbSNP | Ensembl ].
    VAR_046131

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 511511Missing in isoform 2. 1 PublicationVSP_035131Add
    BLAST
    Alternative sequencei511 – 58373IMFVQ…VPGSG → NRVCTLLLVEPHSPAWAPWL GWGWGRGASTCFQQGTQGGG QCLLQAGPRGGTHGRGAWPD ASCCLLGEDSQLL in isoform 3. 1 PublicationVSP_035132Add
    BLAST
    Alternative sequencei512 – 5154MFVQ → LGDE in isoform 4. 1 PublicationVSP_035133
    Alternative sequencei516 – 1504989Missing in isoform 4. 1 PublicationVSP_035134Add
    BLAST
    Alternative sequencei584 – 1504921Missing in isoform 3. 1 PublicationVSP_035135Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082516 mRNA. Translation: AAC33104.1.
    AB023192 mRNA. Translation: BAA76819.1. Different initiation.
    AK291398 mRNA. Translation: BAF84087.1.
    AL117432 mRNA. Translation: CAB55920.1.
    AC006208 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65229.1.
    BC038102 mRNA. Translation: AAH38102.1.
    BC054494 mRNA. Translation: AAH54494.1.
    BC056900 mRNA. Translation: AAH56900.1.
    AF058290 mRNA. Translation: AAC33321.1.
    CCDSiCCDS33767.1. [Q9Y2I1-1]
    CCDS63651.1. [Q9Y2I1-4]
    CCDS63652.1. [Q9Y2I1-3]
    PIRiT17230.
    RefSeqiNP_001263222.1. NM_001276293.1.
    NP_001263223.1. NM_001276294.1.
    NP_009115.2. NM_007184.3.
    UniGeneiHs.435290.

    Genome annotation databases

    EnsembliENST00000345716; ENSP00000339958; ENSG00000010322. [Q9Y2I1-1]
    ENST00000420808; ENSP00000392484; ENSG00000010322. [Q9Y2I1-4]
    ENST00000479054; ENSP00000418232; ENSG00000010322. [Q9Y2I1-1]
    GeneIDi11188.
    KEGGihsa:11188.
    UCSCiuc003ded.4. human. [Q9Y2I1-1]
    uc031sad.1. human. [Q9Y2I1-4]

    Polymorphism databases

    DMDMi296439287.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082516 mRNA. Translation: AAC33104.1 .
    AB023192 mRNA. Translation: BAA76819.1 . Different initiation.
    AK291398 mRNA. Translation: BAF84087.1 .
    AL117432 mRNA. Translation: CAB55920.1 .
    AC006208 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65229.1 .
    BC038102 mRNA. Translation: AAH38102.1 .
    BC054494 mRNA. Translation: AAH54494.1 .
    BC056900 mRNA. Translation: AAH56900.1 .
    AF058290 mRNA. Translation: AAC33321.1 .
    CCDSi CCDS33767.1. [Q9Y2I1-1 ]
    CCDS63651.1. [Q9Y2I1-4 ]
    CCDS63652.1. [Q9Y2I1-3 ]
    PIRi T17230.
    RefSeqi NP_001263222.1. NM_001276293.1.
    NP_001263223.1. NM_001276294.1.
    NP_009115.2. NM_007184.3.
    UniGenei Hs.435290.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3P0C X-ray 2.27 A/B 18-124 [» ]
    ProteinModelPortali Q9Y2I1.
    SMRi Q9Y2I1. Positions 18-123, 212-468.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116358. 7 interactions.
    IntActi Q9Y2I1. 13 interactions.
    STRINGi 9606.ENSP00000339958.

    Chemistry

    ChEMBLi CHEMBL3923.

    PTM databases

    PhosphoSitei Q9Y2I1.

    Polymorphism databases

    DMDMi 296439287.

    Proteomic databases

    MaxQBi Q9Y2I1.
    PaxDbi Q9Y2I1.
    PRIDEi Q9Y2I1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345716 ; ENSP00000339958 ; ENSG00000010322 . [Q9Y2I1-1 ]
    ENST00000420808 ; ENSP00000392484 ; ENSG00000010322 . [Q9Y2I1-4 ]
    ENST00000479054 ; ENSP00000418232 ; ENSG00000010322 . [Q9Y2I1-1 ]
    GeneIDi 11188.
    KEGGi hsa:11188.
    UCSCi uc003ded.4. human. [Q9Y2I1-1 ]
    uc031sad.1. human. [Q9Y2I1-4 ]

    Organism-specific databases

    CTDi 11188.
    GeneCardsi GC03P052489.
    HGNCi HGNC:18006. NISCH.
    HPAi HPA023189.
    MIMi 615507. gene.
    neXtProti NX_Q9Y2I1.
    PharmGKBi PA31635.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269110.
    HOVERGENi HBG108189.
    InParanoidi Q9Y2I1.
    OMAi GNIEWAS.
    OrthoDBi EOG70ZZMH.
    PhylomeDBi Q9Y2I1.
    TreeFami TF320547.

    Enzyme and pathway databases

    SignaLinki Q9Y2I1.

    Miscellaneous databases

    ChiTaRSi NISCH. human.
    GeneWikii NISCH.
    GenomeRNAii 11188.
    NextBioi 42587.
    PROi Q9Y2I1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2I1.
    Bgeei Q9Y2I1.
    CleanExi HS_NISCH.
    Genevestigatori Q9Y2I1.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR001611. Leu-rich_rpt.
    IPR001683. Phox.
    [Graphical view ]
    Pfami PF13855. LRR_8. 1 hit.
    PF00787. PX. 1 hit.
    [Graphical view ]
    SMARTi SM00312. PX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64268. SSF64268. 1 hit.
    PROSITEi PS51450. LRR. 6 hits.
    PS50195. PX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, VARIANTS ILE-299 AND VAL-1056.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION, TISSUE SPECIFICITY, VARIANT ILE-299.
    3. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-299 AND VAL-1056.
      Tissue: Brain.
    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] (ISOFORM 1), VARIANTS ILE-299 AND VAL-1056.
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT VAL-1056.
      Tissue: Testis.
    6. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ILE-299 AND VAL-1056.
    8. "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 1), VARIANTS ILE-299 AND VAL-1056.
      Tissue: Eye, PNS and Testis.
    9. "Characterization of a partial cDNA clone detected by imidazoline receptor-selective antisera."
      Ivanov T.R., Jones J.C., Dontenwill M., Bousquet P., Piletz J.E.
      J. Auton. Nerv. Syst. 72:98-110(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 469-1063 (ISOFORM 1), TISSUE SPECIFICITY, VARIANT VAL-1056.
      Tissue: Hippocampus.
    10. "Insulin receptor substrate 4 associates with the protein IRAS."
      Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.
      J. Biol. Chem. 277:19439-19447(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB2; IRS4 AND PIK3R1, SUBCELLULAR LOCATION.
    11. Cited for: FUNCTION.
    12. "IRAS, the human homologue of Nischarin, prolongs survival of transfected PC12 cells."
      Dontenwill M., Pascal G., Piletz J.E., Chen M., Baldwin J., Ronde P., Dupuy L., Urosevic D., Greney H., Takeda K., Bousquet P.
      Cell Death Differ. 10:933-935(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Human Nischarin/imidazoline receptor antisera-selected protein is targeted to the endosomes by a combined action of a PX domain and a coiled-coil region."
      Lim K.-P., Hong W.
      J. Biol. Chem. 279:54770-54782(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH ITGA5, MUTAGENESIS OF ARG-49 AND TYR-50, SUBCELLULAR LOCATION.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Integrin-binding protein nischarin interacts with tumor suppressor liver kinase B1 (LKB1) to regulate cell migration of breast epithelial cells."
      Jain P., Baranwal S., Dong S., Struckhoff A.P., Worthylake R.A., Alahari S.K.
      J. Biol. Chem. 288:15495-15509(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STK11, SUBCELLULAR LOCATION.
    18. "Crystal structure of nischarin PX-domain."
      Structural genomics consortium (SGC)
      Submitted (OCT-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 18-124.

    Entry informationi

    Entry nameiNISCH_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2I1
    Secondary accession number(s): C9J245
    , Q6PGP3, Q6PIB4, Q7L8M3, Q7Z2X6, Q9UES6, Q9UEU4, Q9UFW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 100 of the entry and version 3 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 3
      Human chromosome 3: 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