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Protein

Nischarin

Gene

Nisch

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

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. Suppresses Rac1-stimulated cell migration by interacting with PAK1 and inhibiting its kinase activity. Also blocks Pak-independent Rac signaling by interacting with RAC1 and inhibiting Rac1-stimulated NF-kB response element and cyclin D1 promoter activation. Inhibits also LIMK1 kinase activity by reducing LIMK1 'Tyr-508' phosphorylation. Inhibits Rac-induced cell migration and invasion in breast and colon epithelial cells. Inhibits lamellipodia formation, when overexpressed. Plays a role in protection against apoptosis (By similarity). Involved in association with IRS4 in the enhancement of insulin activation of MAPK1 and MAPK3 (By similarity). When overexpressed, induces a redistribution of cell surface ITGA5 integrin to intracellular endosomal structures (By similarity).By similarity6 Publications

GO - Molecular functioni

  • integrin binding Source: MGI
  • phosphatidylinositol binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Nischarin
Alternative name(s):
Imidazoline receptor 1
Short name:
I-1
Short name:
IR1
Imidazoline receptor I-1-like protein
Imidazoline-1 receptor
Short name:
I1R
Gene namesi
Name:Nisch
Synonyms:Kiaa0975
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1928323. Nisch.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • early endosome Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
  • recycling endosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15931593NischarinPRO_0000348266Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei543 – 5431PhosphoserineCombined sources
Modified residuei545 – 5451PhosphoserineCombined sources
Modified residuei548 – 5481PhosphoserineCombined sources
Modified residuei1371 – 13711PhosphothreonineCombined sources
Modified residuei1373 – 13731PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ80TM9.
MaxQBiQ80TM9.
PaxDbiQ80TM9.
PRIDEiQ80TM9.

PTM databases

iPTMnetiQ80TM9.
PhosphoSiteiQ80TM9.

Expressioni

Tissue specificityi

Highly expressed in brain and kidney. Moderately expressed in heart, liver, lung and skeletal muscle. Not detected in spleen and testis.1 Publication

Developmental stagei

Expressed in embryo at 7 day dpc onwards.1 Publication

Gene expression databases

BgeeiQ80TM9.
ExpressionAtlasiQ80TM9. baseline and differential.
GenevisibleiQ80TM9. MM.

Interactioni

Subunit structurei

Homooligomer (By similarity). Interacts with GRB2 (By similarity). Interacts with PIK3R1; probably associates with the PI3-kinase complex (By similarity). Interacts with IRS4 (By similarity). 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. Interacts with LIMK1 (via PDZ and kinase domain); this interaction is direct. Interacts with LIMK2; this interaction depends on LIMK2 activity. Interacts with RAC1 (activated state). Interacts with STK11; this interaction may increase STK11 activity (By similarity).By similarity

GO - Molecular functioni

  • integrin binding Source: MGI

Protein-protein interaction databases

BioGridi211089. 1 interaction.
IntActiQ80TM9. 1 interaction.
MINTiMINT-4128927.
STRINGi10090.ENSMUSP00000022469.

Structurei

3D structure databases

ProteinModelPortaliQ80TM9.
SMRiQ80TM9. Positions 19-122.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 122111PXPROSITE-ProRule annotationAdd
BLAST
Repeati290 – 31122LRR 1Add
BLAST
Repeati313 – 33422LRR 2Add
BLAST
Repeati335 – 35622LRR 3Add
BLAST
Repeati358 – 37922LRR 4Add
BLAST
Repeati380 – 40122LRR 5Add
BLAST
Repeati405 – 42622LRR 6Add
BLAST
Repeati1081 – 108661
Repeati1087 – 109262
Repeati1093 – 109863
Repeati1099 – 110464
Repeati1105 – 111065
Repeati1111 – 111666
Repeati1123 – 112867
Repeati1129 – 113468
Repeati1135 – 114069
Repeati1141 – 1146610

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 134134Necessary for binding to phosphoinositide-3-P; not sufficient for targeting to endosomesBy similarityAdd
BLAST
Regioni121 – 695575Necessary for homooligomerization and targeting to endosomesBy similarityAdd
BLAST
Regioni246 – 869624Interaction with PAK1Add
BLAST
Regioni661 – 869209Interaction with LIMKAdd
BLAST
Regioni709 – 80799Interaction with ITGA5Add
BLAST
Regioni1081 – 11466610 X 6 AA tandem repeat of A-E-A-P-A-AAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili624 – 69471Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi631 – 69161Glu-richAdd
BLAST
Compositional biasi1041 – 1193153Ala/Pro-richAdd
BLAST

Domaini

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

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

eggNOGiKOG1259. Eukaryota.
ENOG410XQUS. LUCA.
GeneTreeiENSGT00530000063625.
HOVERGENiHBG108189.
InParanoidiQ80TM9.
OMAiYSGNIEW.
OrthoDBiEOG70ZZMH.
PhylomeDBiQ80TM9.
TreeFamiTF320547.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR001683. Phox.
[Graphical view]
PfamiPF12799. LRR_4. 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 (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80TM9-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MAAATLSFGP EREAEPAKEA RVVGSELVDT YTVYVIQVTD GNHEWTIKHR
60 70 80 90 100
YSDFHDLHEK LVAERKIDKS LLPPKKIIGK NSRSLVEKRE RDLEVYLQTL
110 120 130 140 150
LTTFPDVAPR VLAHFLHFHL YEVNGVTAAL AEELFEKGEQ LLGAGEVFAI
160 170 180 190 200
RPLQLYAITE QLQQGKPTCA SGDAKTDLGH ILDFTCRLKY LKVSGTEGPF
210 220 230 240 250
GTSNIKEQLL PFDLSIFKSL HQVEISHCDA KHIRGLVTSK PTLATMSVRF
260 270 280 290 300
SATSMKEVLA PEASEFDEWE PEGTATLGGP VTAIIPTWQA LTTLDLSHNS
310 320 330 340 350
ICEIDESVKL IPKIEYLDLS HNGLRVVDNL QHLYNLVHLD LSYNKLSSLE
360 370 380 390 400
GVHTKLGNVK TLNLAGNFLE SLSGLHKLYS LVNVDLRDNR IEQLDEVKSI
410 420 430 440 450
GSLPCLERLT LLNNPLSIIP DYRTKVLSQF GERASEICLD DVATTEKELD
460 470 480 490 500
TVEVLKAIQK AKDVKSKLSN TEKKAGEDFR LPPAPCIRPG GSPPAAPASA
510 520 530 540 550
SLPQPILSNQ GIMFVQEEAL ASSLSSTDSL PPEDHRPIAR ACSDSLESIP
560 570 580 590 600
AGQVASDDLR DVPGAVGGVS PDHAEPEVQV VPGSGQIIFL PFTCIGYTAT
610 620 630 640 650
NQDFIQRLST LIRQAIERQL PAWIEAANQR EEAHGEQGEE EEEEEEEEDV
660 670 680 690 700
AENRYFEMGP PDAEEEEGSG QGEEDEEDED EEAEEERLAL EWALGADEDF
710 720 730 740 750
LLEHIRILKV LWCFLIHVQG SIRQFAACLV LTDFGIAVFE IPHQESRGSS
760 770 780 790 800
QHILSSLRFV FCFPHGDLTE FGFLMPELCL VLKVRHSENT LFIISDAANL
810 820 830 840 850
HEFHADLRSC FAPQHMAMLC SPILYGSHTT LQEFLRQLLT FYKVAGGSQE
860 870 880 890 900
RSQGCFPVYL VYSDKRMVQT PAGDYSGNIE WASCTLCSAV RRSCCAPSEA
910 920 930 940 950
VKSAAIPYWL LLTSQHLNVI KADFNPMPNR GTHNCRNRNS FKLSRVPLST
960 970 980 990 1000
VLLDPTRSCT QPRGAFADGH VLELLVGYRF VTAIFVLPHE KFHFLRVYNQ
1010 1020 1030 1040 1050
LRASLQDLKT VVISKNPSAK PRNQPAKSRA SAEQRLQETP ADAPAPAAVP
1060 1070 1080 1090 1100
PTASAPAPAE ALAPDLAPVQ APGEDRGLTS AEAPAAAEAP AAAEAPAAAE
1110 1120 1130 1140 1150
APAAAEAPAA AEAPAAAEAP APAEAPAAAE APAAAEAPAA AEAPAAAEAP
1160 1170 1180 1190 1200
ASAEAPAPNQ APAPARGPAP ARGPAPAGGP APAEALAQAE VPAQYPSERL
1210 1220 1230 1240 1250
IQSTSEENQI PSHLPVCPSL QHIARLRGRA IIDLFHNSIA EVENEELRHL
1260 1270 1280 1290 1300
LWSSVVFYQT PGLEVTACVL LSSKAVYFIL HDGLRRYFSE PLQDFWHQKN
1310 1320 1330 1340 1350
TDYNNSPFHV SQCFVLKLSD LQSVNVGLFD QYFRLTGSSP TQVVTCLTRD
1360 1370 1380 1390 1400
SYLTHCFLQH LMLVLSSLER TPSPEPVDKD FYSEFGDKNT GKMENYELIH
1410 1420 1430 1440 1450
SSRVKFTYPS EEEVGDLTYI VAQKMADPAK NPALSILLYI QAFQVVTPHL
1460 1470 1480 1490 1500
GRGRGPLRPK TLLLTSAEIF LLDEDYIHYP LPEFAKEPPQ RDRYRLDDGR
1510 1520 1530 1540 1550
RVRDLDRVLM GYYPYPQALT LVFDDTQGHD LMGSVTLDHF GEMPGGPGRV
1560 1570 1580 1590
GQGREVQWQV FVPSAESREK LISLLARQWE ALCGRELPVE LTG
Length:1,593
Mass (Da):175,012
Last modified:September 2, 2008 - v2
Checksum:i90B407A165A4C1F8
GO
Isoform 2 (identifier: Q80TM9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     348-500: Missing.

Show »
Length:1,440
Mass (Da):158,425
Checksum:i8FFFBF697A5BEA01
GO
Isoform 3 (identifier: Q80TM9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-245: Missing.

Show »
Length:1,348
Mass (Da):147,611
Checksum:i9F92EED9E2342519
GO
Isoform 4 (identifier: Q80TM9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     437-472: ICLDDVATTEKELDTVEVLKAIQKAKDVKSKLSNTE → VSPRSSSRAQRDWQGKPSLSAKADRGKAVHSVLVFF
     473-1593: Missing.

Show »
Length:472
Mass (Da):52,609
Checksum:i115AB01516952992
GO
Isoform 5 (identifier: Q80TM9-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     332-334: HLY → ATS
     335-1593: Missing.

Note: No experimental confirmation available.
Show »
Length:334
Mass (Da):37,131
Checksum:i00B86B5695E19BB7
GO
Isoform 6 (identifier: Q80TM9-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     513-516: MFVQ → LGDE
     517-1593: Missing.

Show »
Length:516
Mass (Da):57,033
Checksum:i95AF24DEBE8B6BF9
GO
Isoform 7 (identifier: Q80TM9-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-153: EVNGVTAALAEELFEKGEQLLGAGEVFAIRPL → VSSFGALCFAYEPTATKAVGLGFEETQTGPWP
     154-1593: Missing.

Show »
Length:153
Mass (Da):17,328
Checksum:i4E902C8FBC992DE7
GO

Sequence cautioni

The sequence AAH03270.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI08365.1 differs from that shown. Reason: Frameshift at position 1550. Curated
The sequence AAK52087.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC65694.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti607 – 6071R → P in BAC65694 (PubMed:12693553).Curated
Sequence conflicti1123 – 11286Missing in BAC65694 (PubMed:12693553).Curated
Sequence conflicti1172 – 11721R → RGPAPAG in AAG42100 (PubMed:11121431).Curated
Sequence conflicti1518 – 15181A → G in AAK52087 (Ref. 6) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 245245Missing in isoform 3. 1 PublicationVSP_035136Add
BLAST
Alternative sequencei122 – 15332EVNGV…AIRPL → VSSFGALCFAYEPTATKAVG LGFEETQTGPWP in isoform 7. 1 PublicationVSP_035137Add
BLAST
Alternative sequencei154 – 15931440Missing in isoform 7. 1 PublicationVSP_035138Add
BLAST
Alternative sequencei332 – 3343HLY → ATS in isoform 5. 1 PublicationVSP_035139
Alternative sequencei335 – 15931259Missing in isoform 5. 1 PublicationVSP_035140Add
BLAST
Alternative sequencei348 – 500153Missing in isoform 2. 1 PublicationVSP_035141Add
BLAST
Alternative sequencei437 – 47236ICLDD…LSNTE → VSPRSSSRAQRDWQGKPSLS AKADRGKAVHSVLVFF in isoform 4. 1 PublicationVSP_035142Add
BLAST
Alternative sequencei473 – 15931121Missing in isoform 4. 1 PublicationVSP_035143Add
BLAST
Alternative sequencei513 – 5164MFVQ → LGDE in isoform 6. 1 PublicationVSP_035144
Alternative sequencei517 – 15931077Missing in isoform 6. 1 PublicationVSP_035145Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF315344 mRNA. Translation: AAG42100.1.
AK122412 mRNA. Translation: BAC65694.1. Different initiation.
AK036043 mRNA. Translation: BAC29286.1.
AK080441 mRNA. Translation: BAC37917.1.
AK086880 mRNA. Translation: BAC39757.1.
AC108416 Genomic DNA. No translation available.
AC154446 Genomic DNA. No translation available.
BC003270 mRNA. Translation: AAH03270.1. Different initiation.
BC108364 mRNA. Translation: AAI08365.1. Frameshift.
AY032852 mRNA. Translation: AAK52087.1. Different initiation.
AF144133 mRNA. Translation: AAD31521.1.
CCDSiCCDS36853.1. [Q80TM9-1]
RefSeqiNP_073147.2. NM_022656.2. [Q80TM9-1]
XP_006519417.2. XM_006519354.2. [Q80TM9-6]
UniGeneiMm.298728.

Genome annotation databases

EnsembliENSMUST00000022469; ENSMUSP00000022469; ENSMUSG00000021910. [Q80TM9-1]
ENSMUST00000164989; ENSMUSP00000126982; ENSMUSG00000021910. [Q80TM9-5]
ENSMUST00000165981; ENSMUSP00000130210; ENSMUSG00000021910. [Q80TM9-4]
ENSMUST00000168206; ENSMUSP00000132842; ENSMUSG00000021910. [Q80TM9-3]
ENSMUST00000171735; ENSMUSP00000127132; ENSMUSG00000021910. [Q80TM9-7]
ENSMUST00000172142; ENSMUSP00000132413; ENSMUSG00000021910. [Q80TM9-6]
GeneIDi64652.
KEGGimmu:64652.
UCSCiuc007swy.1. mouse. [Q80TM9-1]
uc007sxa.1. mouse. [Q80TM9-6]
uc007sxb.1. mouse. [Q80TM9-4]
uc007sxc.1. mouse. [Q80TM9-7]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF315344 mRNA. Translation: AAG42100.1.
AK122412 mRNA. Translation: BAC65694.1. Different initiation.
AK036043 mRNA. Translation: BAC29286.1.
AK080441 mRNA. Translation: BAC37917.1.
AK086880 mRNA. Translation: BAC39757.1.
AC108416 Genomic DNA. No translation available.
AC154446 Genomic DNA. No translation available.
BC003270 mRNA. Translation: AAH03270.1. Different initiation.
BC108364 mRNA. Translation: AAI08365.1. Frameshift.
AY032852 mRNA. Translation: AAK52087.1. Different initiation.
AF144133 mRNA. Translation: AAD31521.1.
CCDSiCCDS36853.1. [Q80TM9-1]
RefSeqiNP_073147.2. NM_022656.2. [Q80TM9-1]
XP_006519417.2. XM_006519354.2. [Q80TM9-6]
UniGeneiMm.298728.

3D structure databases

ProteinModelPortaliQ80TM9.
SMRiQ80TM9. Positions 19-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211089. 1 interaction.
IntActiQ80TM9. 1 interaction.
MINTiMINT-4128927.
STRINGi10090.ENSMUSP00000022469.

PTM databases

iPTMnetiQ80TM9.
PhosphoSiteiQ80TM9.

Proteomic databases

EPDiQ80TM9.
MaxQBiQ80TM9.
PaxDbiQ80TM9.
PRIDEiQ80TM9.

Protocols and materials databases

DNASUi64652.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022469; ENSMUSP00000022469; ENSMUSG00000021910. [Q80TM9-1]
ENSMUST00000164989; ENSMUSP00000126982; ENSMUSG00000021910. [Q80TM9-5]
ENSMUST00000165981; ENSMUSP00000130210; ENSMUSG00000021910. [Q80TM9-4]
ENSMUST00000168206; ENSMUSP00000132842; ENSMUSG00000021910. [Q80TM9-3]
ENSMUST00000171735; ENSMUSP00000127132; ENSMUSG00000021910. [Q80TM9-7]
ENSMUST00000172142; ENSMUSP00000132413; ENSMUSG00000021910. [Q80TM9-6]
GeneIDi64652.
KEGGimmu:64652.
UCSCiuc007swy.1. mouse. [Q80TM9-1]
uc007sxa.1. mouse. [Q80TM9-6]
uc007sxb.1. mouse. [Q80TM9-4]
uc007sxc.1. mouse. [Q80TM9-7]

Organism-specific databases

CTDi11188.
MGIiMGI:1928323. Nisch.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1259. Eukaryota.
ENOG410XQUS. LUCA.
GeneTreeiENSGT00530000063625.
HOVERGENiHBG108189.
InParanoidiQ80TM9.
OMAiYSGNIEW.
OrthoDBiEOG70ZZMH.
PhylomeDBiQ80TM9.
TreeFamiTF320547.

Miscellaneous databases

ChiTaRSiNisch. mouse.
PROiQ80TM9.
SOURCEiSearch...

Gene expression databases

BgeeiQ80TM9.
ExpressionAtlasiQ80TM9. baseline and differential.
GenevisibleiQ80TM9. MM.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR001683. Phox.
[Graphical view]
PfamiPF12799. LRR_4. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nischarin, a novel protein that interacts with the integrin alpha5 subunit and inhibits cell migration."
    Alahari S.K., Lee J.W., Juliano R.L.
    J. Cell Biol. 151:1141-1154(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH ITGA5, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    Strain: ICR.
    Tissue: Brain.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "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] (ISOFORMS 4; 5 AND 7).
    Strain: C57BL/6J.
    Tissue: Cerebellum and Lung.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 215-1593 (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Colon and Mammary tumor.
  6. Bailey T.L., Smith D.R., McGaugh B.D., Mitchell J.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1238-1593 (ISOFORM 1).
    Tissue: Carcinoma.
  7. Cain D., Carter J., McLean W., Robbins L.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1386-1593 (ISOFORM 1).
    Tissue: Lung.
  8. "Nischarin inhibits Rac induced migration and invasion of epithelial cells by affecting signaling cascades involving PAK."
    Alahari S.K.
    Exp. Cell Res. 288:415-424(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "A membrane proximal region of the integrin alpha5 subunit is important for its interaction with nischarin."
    Alahari S.K., Nasrallah H.
    Biochem. J. 377:449-457(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITGA5.
  10. "The integrin-binding protein Nischarin regulates cell migration by inhibiting PAK."
    Alahari S.K., Reddig P.J., Juliano R.L.
    EMBO J. 23:2777-2788(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH ITGA5 AND PAK1, INTERACTION WITH PAK1, SUBCELLULAR LOCATION.
  11. "Regulation of p21-activated kinase-independent Rac1 signal transduction by Nischarin."
    Reddig P.J., Xu D., Juliano R.L.
    J. Biol. Chem. 280:30994-31002(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAC1, SUBCELLULAR LOCATION.
  12. "Nischarin as a functional imidazoline (I1) receptor."
    Zhang J., Abdel-Rahman A.A.
    FEBS Lett. 580:3070-3074(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Nischarin inhibits LIM kinase to regulate cofilin phosphorylation and cell invasion."
    Ding Y., Milosavljevic T., Alahari S.K.
    Mol. Cell. Biol. 28:3742-3756(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH LIMK1 AND PAK1, INTERACTION WITH LIMK1 AND LIMK2.
  15. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543; SER-545; SER-548 AND THR-1371, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiNISCH_MOUSE
AccessioniPrimary (citable) accession number: Q80TM9
Secondary accession number(s): Q2YDV7
, Q8C354, Q8C4X9, Q8CBH0, Q91XW6, Q99LG6, Q9EPW8, Q9WUM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: June 8, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

'Nischarin' means 'slowness of motion' in classic Sanskrit.

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.