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Protein

Nischarin

Gene

NISCH

Organism
Homo sapiens (Human)
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 (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

GO - Biological processi

Complete GO annotation...

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 Componenti: 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

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

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.

Chemistry

DrugBankiDB00697. Tizanidine.

Polymorphism and mutation databases

BioMutaiNISCH.
DMDMi296439287.

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

BgeeiQ9Y2I1.
CleanExiHS_NISCH.
ExpressionAtlasiQ9Y2I1. baseline and differential.
GenevisibleiQ9Y2I1. HS.

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. 10 interactions.
IntActiQ9Y2I1. 13 interactions.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P0CX-ray2.27A/B18-124[»]
ProteinModelPortaliQ9Y2I1.
SMRiQ9Y2I1. Positions 18-123.
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.
GeneTreeiENSGT00530000063625.
HOVERGENiHBG108189.
InParanoidiQ9Y2I1.
OMAiTEFGFLM.
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. AlignAdd to basket

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

        10         20         30         40         50
MATARTFGPE REAEPAKEAR VVGSELVDTY TVYIIQVTDG SHEWTVKHRY
60 70 80 90 100
SDFHDLHEKL VAERKIDKNL LPPKKIIGKN SRSLVEKREK DLEVYLQKLL
110 120 130 140 150
AAFPGVTPRV LAHFLHFHFY EINGITAALA EELFEKGEQL LGAGEVFAIG
160 170 180 190 200
PLQLYAVTEQ LQQGKPTCAS GDAKTDLGHI LDFTCRLKYL KVSGTEGPFG
210 220 230 240 250
TSNIQEQLLP FDLSIFKSLH QVEISHCDAK HIRGLVASKP TLATLSVRFS
260 270 280 290 300
ATSMKEVLVP EASEFDEWEP EGTTLEGPVT AVIPTWQALT TLDLSHNSVS
310 320 330 340 350
EIDESVKLIP KIEFLDLSHN GLLVVDNLQH LYNLVHLDLS YNKLSSLEGL
360 370 380 390 400
HTKLGNIKTL NLAGNLLESL SGLHKLYSLV NLDLRDNRIE QMEEVRSIGS
410 420 430 440 450
LPCLEHVSLL NNPLSIIPDY RTKVLAQFGE RASEVCLDDT VTTEKELDTV
460 470 480 490 500
EVLKAIQKAK EVKSKLSNPE KKGGEDSRLS AAPCIRPSSS PPTVAPASAS
510 520 530 540 550
LPQPILSNQG IMFVQEEALA SSLSSTDSLT PEHQPIAQGC SDSLESIPAG
560 570 580 590 600
QAASDDLRDV PGAVGGASPE HAEPEVQVVP GSGQIIFLPF TCIGYTATNQ
610 620 630 640 650
DFIQRLSTLI RQAIERQLPA WIEAANQREE GQGEQGEEED EEEEEEEDVA
660 670 680 690 700
ENRYFEMGPP DVEEEEGGGQ GEEEEEEEED 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 SPILYGSHTS LQEFLRQLLT FYKVAGGCQE
860 870 880 890 900
RSQGCFPVYL VYSDKRMVQT AAGDYSGNIE WASCTLCSAV RRSCCAPSEA
910 920 930 940 950
VKSAAIPYWL LLTPQHLNVI KADFNPMPNR GTHNCRNRNS FKLSRVPLST
960 970 980 990 1000
VLLDPTRSCT QPRGAFADGH VLELLVGYRF VTAIFVLPHE KFHFLRVYNQ
1010 1020 1030 1040 1050
LRASLQDLKT VVIAKTPGTG GSPQGSFADG QPAERRASND QRPQEVPAEA
1060 1070 1080 1090 1100
LAPAPAEVPA PAPAAASASG PAKTPAPAEA STSALVPEET PVEAPAPPPA
1110 1120 1130 1140 1150
EAPAQYPSEH LIQATSEENQ IPSHLPACPS LRHVASLRGS AIIELFHSSI
1160 1170 1180 1190 1200
AEVENEELRH LMWSSVVFYQ TPGLEVTACV LLSTKAVYFV LHDGLRRYFS
1210 1220 1230 1240 1250
EPLQDFWHQK NTDYNNSPFH ISQCFVLKLS DLQSVNVGLF DQHFRLTGST
1260 1270 1280 1290 1300
PMQVVTCLTR DSYLTHCFLQ HLMVVLSSLE RTPSPEPVDK DFYSEFGNKT
1310 1320 1330 1340 1350
TGKMENYELI HSSRVKFTYP SEEEIGDLTF TVAQKMAEPE KAPALSILLY
1360 1370 1380 1390 1400
VQAFQVGMPP PGCCRGPLRP KTLLLTSSEI FLLDEDCVHY PLPEFAKEPP
1410 1420 1430 1440 1450
QRDRYRLDDG RRVRDLDRVL MGYQTYPQAL TLVFDDVQGH DLMGSVTLDH
1460 1470 1480 1490 1500
FGEVPGGPAR ASQGREVQWQ VFVPSAESRE KLISLLARQW EALCGRELPV

ELTG
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.Curated

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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P0CX-ray2.27A/B18-124[»]
ProteinModelPortaliQ9Y2I1.
SMRiQ9Y2I1. Positions 18-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116358. 10 interactions.
IntActiQ9Y2I1. 13 interactions.

Chemistry

BindingDBiQ9Y2I1.
ChEMBLiCHEMBL3923.
DrugBankiDB00697. Tizanidine.

PTM databases

PhosphoSiteiQ9Y2I1.

Polymorphism and mutation databases

BioMutaiNISCH.
DMDMi296439287.

Proteomic databases

MaxQBiQ9Y2I1.
PaxDbiQ9Y2I1.
PRIDEiQ9Y2I1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi11188.
GeneCardsiGC03P052489.
HGNCiHGNC:18006. NISCH.
HPAiHPA023189.
MIMi615507. gene.
neXtProtiNX_Q9Y2I1.
PharmGKBiPA31635.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG269110.
GeneTreeiENSGT00530000063625.
HOVERGENiHBG108189.
InParanoidiQ9Y2I1.
OMAiTEFGFLM.
OrthoDBiEOG70ZZMH.
PhylomeDBiQ9Y2I1.
TreeFamiTF320547.

Enzyme and pathway databases

SignaLinkiQ9Y2I1.

Miscellaneous databases

ChiTaRSiNISCH. human.
GeneWikiiNISCH.
GenomeRNAii11188.
NextBioi42587.
PROiQ9Y2I1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2I1.
CleanExiHS_NISCH.
ExpressionAtlasiQ9Y2I1. baseline and differential.
GenevisibleiQ9Y2I1. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 107 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

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 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.