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Q9Y2I1

- NISCH_HUMAN

UniProt

Q9Y2I1 - NISCH_HUMAN

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Protein
Nischarin
Gene
NISCH, IRAS, KIAA0975
Organism
Homo sapiens (Human)
Status
Reviewed - 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.5 Publications

GO - Molecular functioni

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

GO - Biological processi

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

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 15041503Nischarin
PRO_0000348265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei541 – 5411Phosphoserine By 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.3 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. 10 interactions.
STRINGi9606.ENSP00000339958.

Structurei

Secondary structure

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.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 133132Necessary for binding to phosphoinositide-3-P; not sufficient for targeting to endosomes
Add
BLAST
Regioni120 – 695576Necessary for homooligomerization and targeting to endosomes
Add
BLAST
Regioni245 – 869625Interaction with PAK1 By similarity
Add
BLAST
Regioni660 – 869210Interaction with LIMK By similarity
Add
BLAST
Regioni709 – 80799Interaction with ITGA5 By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili634 – 69562 Reviewed prediction
Add
BLAST

Compositional bias

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

Domaini

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

Sequence similaritiesi

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.

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.
VSP_035131Add
BLAST
Alternative sequencei511 – 58373IMFVQ…VPGSG → NRVCTLLLVEPHSPAWAPWL GWGWGRGASTCFQQGTQGGG QCLLQAGPRGGTHGRGAWPD ASCCLLGEDSQLL in isoform 3.
VSP_035132Add
BLAST
Alternative sequencei512 – 5154MFVQ → LGDE in isoform 4.
VSP_035133
Alternative sequencei516 – 1504989Missing in isoform 4.
VSP_035134Add
BLAST
Alternative sequencei584 – 1504921Missing in isoform 3.
VSP_035135Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti927 – 9271M → I in AAH56900. 1 Publication
Sequence conflicti1023 – 10231P → A in BAA76819. 1 Publication
Sequence conflicti1123 – 11231S → P in AAH38102. 1 Publication
Sequence conflicti1382 – 13821L → F in AAH54494. 1 Publication

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. 10 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

« 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: September 3, 2014
This is version 99 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

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