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Q9Y2I1 (NISCH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NISCH
Synonyms:IRAS, KIAA0975
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.11 Ref.12 Ref.13

Subunit structure

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. Ref.10 Ref.13 Ref.17

Subcellular location

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. Ref.1 Ref.10 Ref.12 Ref.13 Ref.17

Tissue specificity

Isoform 1, isoform 3 and isoform 4 are expressed in brain. Isoform 1 is expressed in endocrine tissues. Ref.2 Ref.9

Domain

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

Sequence similarities

Contains 6 LRR (leucine-rich) repeats.

Contains 1 PX (phox homology) domain.

Sequence caution

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

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCell membrane
Cytoplasm
Endosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Leucine-rich repeat
Repeat
   Molecular functionReceptor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRac protein signal transduction

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

glucose metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

norepinephrine secretion

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

regulation of synaptic transmission, GABAergic

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from direct assay PubMed 15028622. Source: BHF-UCL

early endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 15028622. Source: BHF-UCL

recycling endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionG-protein coupled amine receptor activity

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2I1-1)

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.
Isoform 2 (identifier: Q9Y2I1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-511: Missing.
Isoform 3 (identifier: Q9Y2I1-3)

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.
Isoform 4 (identifier: Q9Y2I1-4)

Also known as: IRAS-S;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 15041503Nischarin
PRO_0000348265

Regions

Domain11 – 121111PX
Repeat288 – 30922LRR 1
Repeat311 – 33222LRR 2
Repeat333 – 35422LRR 3
Repeat356 – 37722LRR 4
Repeat378 – 39922LRR 5
Repeat403 – 42422LRR 6
Region2 – 133132Necessary for binding to phosphoinositide-3-P; not sufficient for targeting to endosomes
Region120 – 695576Necessary for homooligomerization and targeting to endosomes
Region245 – 869625Interaction with PAK1 By similarity
Region660 – 869210Interaction with LIMK By similarity
Region709 – 80799Interaction with ITGA5 By similarity
Coiled coil634 – 69562 Potential
Compositional bias629 – 69163Glu-rich
Compositional bias1048 – 110457Ala/Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.14
Modified residue5411Phosphoserine By similarity
Modified residue12841Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 511511Missing in isoform 2.
VSP_035131
Alternative sequence511 – 58373IMFVQ…VPGSG → NRVCTLLLVEPHSPAWAPWL GWGWGRGASTCFQQGTQGGG QCLLQAGPRGGTHGRGAWPD ASCCLLGEDSQLL in isoform 3.
VSP_035132
Alternative sequence512 – 5154MFVQ → LGDE in isoform 4.
VSP_035133
Alternative sequence516 – 1504989Missing in isoform 4.
VSP_035134
Alternative sequence584 – 1504921Missing in isoform 3.
VSP_035135
Natural variant2991V → I. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7 Ref.8
Corresponds to variant rs9856575 [ dbSNP | Ensembl ].
VAR_046130
Natural variant10561A → V. Ref.1 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.9
Corresponds to variant rs887515 [ dbSNP | Ensembl ].
VAR_046131

Experimental info

Mutagenesis491R → A: Inhibits targeting to endosomes. Ref.13
Mutagenesis501Y → A: Inhibits targeting to endosomes. Ref.13
Sequence conflict9271M → I in AAH56900. Ref.8
Sequence conflict10231P → A in BAA76819. Ref.3
Sequence conflict11231S → P in AAH38102. Ref.8
Sequence conflict13821L → F in AAH54494. Ref.8

Secondary structure

................ 1504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (IRAS-1) (IRAS-M) [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 7761C7DA1FDC4E53

FASTA1,504166,629
        10         20         30         40         50         60 
MATARTFGPE REAEPAKEAR VVGSELVDTY TVYIIQVTDG SHEWTVKHRY SDFHDLHEKL 

        70         80         90        100        110        120 
VAERKIDKNL LPPKKIIGKN SRSLVEKREK DLEVYLQKLL AAFPGVTPRV LAHFLHFHFY 

       130        140        150        160        170        180 
EINGITAALA EELFEKGEQL LGAGEVFAIG PLQLYAVTEQ LQQGKPTCAS GDAKTDLGHI 

       190        200        210        220        230        240 
LDFTCRLKYL KVSGTEGPFG TSNIQEQLLP FDLSIFKSLH QVEISHCDAK HIRGLVASKP 

       250        260        270        280        290        300 
TLATLSVRFS ATSMKEVLVP EASEFDEWEP EGTTLEGPVT AVIPTWQALT TLDLSHNSVS 

       310        320        330        340        350        360 
EIDESVKLIP KIEFLDLSHN GLLVVDNLQH LYNLVHLDLS YNKLSSLEGL HTKLGNIKTL 

       370        380        390        400        410        420 
NLAGNLLESL SGLHKLYSLV NLDLRDNRIE QMEEVRSIGS LPCLEHVSLL NNPLSIIPDY 

       430        440        450        460        470        480 
RTKVLAQFGE RASEVCLDDT VTTEKELDTV EVLKAIQKAK EVKSKLSNPE KKGGEDSRLS 

       490        500        510        520        530        540 
AAPCIRPSSS PPTVAPASAS LPQPILSNQG IMFVQEEALA SSLSSTDSLT PEHQPIAQGC 

       550        560        570        580        590        600 
SDSLESIPAG QAASDDLRDV PGAVGGASPE HAEPEVQVVP GSGQIIFLPF TCIGYTATNQ 

       610        620        630        640        650        660 
DFIQRLSTLI RQAIERQLPA WIEAANQREE GQGEQGEEED EEEEEEEDVA ENRYFEMGPP 

       670        680        690        700        710        720 
DVEEEEGGGQ GEEEEEEEED EEAEEERLAL EWALGADEDF LLEHIRILKV LWCFLIHVQG 

       730        740        750        760        770        780 
SIRQFAACLV LTDFGIAVFE IPHQESRGSS QHILSSLRFV FCFPHGDLTE FGFLMPELCL 

       790        800        810        820        830        840 
VLKVRHSENT LFIISDAANL HEFHADLRSC FAPQHMAMLC SPILYGSHTS LQEFLRQLLT 

       850        860        870        880        890        900 
FYKVAGGCQE RSQGCFPVYL VYSDKRMVQT AAGDYSGNIE WASCTLCSAV RRSCCAPSEA 

       910        920        930        940        950        960 
VKSAAIPYWL LLTPQHLNVI KADFNPMPNR GTHNCRNRNS FKLSRVPLST VLLDPTRSCT 

       970        980        990       1000       1010       1020 
QPRGAFADGH VLELLVGYRF VTAIFVLPHE KFHFLRVYNQ LRASLQDLKT VVIAKTPGTG 

      1030       1040       1050       1060       1070       1080 
GSPQGSFADG QPAERRASND QRPQEVPAEA LAPAPAEVPA PAPAAASASG PAKTPAPAEA 

      1090       1100       1110       1120       1130       1140 
STSALVPEET PVEAPAPPPA EAPAQYPSEH LIQATSEENQ IPSHLPACPS LRHVASLRGS 

      1150       1160       1170       1180       1190       1200 
AIIELFHSSI AEVENEELRH LMWSSVVFYQ TPGLEVTACV LLSTKAVYFV LHDGLRRYFS 

      1210       1220       1230       1240       1250       1260 
EPLQDFWHQK NTDYNNSPFH ISQCFVLKLS DLQSVNVGLF DQHFRLTGST PMQVVTCLTR 

      1270       1280       1290       1300       1310       1320 
DSYLTHCFLQ HLMVVLSSLE RTPSPEPVDK DFYSEFGNKT TGKMENYELI HSSRVKFTYP 

      1330       1340       1350       1360       1370       1380 
SEEEIGDLTF TVAQKMAEPE KAPALSILLY VQAFQVGMPP PGCCRGPLRP KTLLLTSSEI 

      1390       1400       1410       1420       1430       1440 
FLLDEDCVHY PLPEFAKEPP QRDRYRLDDG RRVRDLDRVL MGYQTYPQAL TLVFDDVQGH 

      1450       1460       1470       1480       1490       1500 
DLMGSVTLDH FGEVPGGPAR ASQGREVQWQ VFVPSAESRE KLISLLARQW EALCGRELPV 


ELTG 

« Hide

Isoform 2 [UniParc].

Checksum: E0415818937AA523
Show »

FASTA993110,194
Isoform 3 (IRAS-L) [UniParc].

Checksum: 83CED19440961191
Show »

FASTA58363,997
Isoform 4 (IRAS-S) [UniParc].

Checksum: B623BE4D42BBA51C
Show »

FASTA51556,867

References

« Hide 'large scale' references
[1]"Imidazoline receptor antisera-selected (IRAS) cDNA: cloning and characterization."
Piletz J.E., Ivanov T.R., Sharp J.D., Ernsberger P., Chang C.-H., Pickard R.T., Gold G., Roth B., Zhu H., Jones J.C., Baldwin J., Reis D.J.
DNA Cell Biol. 19:319-329(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, VARIANTS ILE-299 AND VAL-1056.
[2]"IRAS splice variants."
Piletz J.E., Deleersnijder W., Roth B.L., Ernsberger P., Zhu H., Ziegler D.
Ann. N. Y. Acad. Sci. 1009:419-426(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"IRAS is an anti-apoptotic protein."
Dontenwill M., Piletz J.E., Chen M., Baldwin J., Pascal G., Ronde P., Dupuy L., Greney H., Takeda K., Bousquetd P.
Ann. N. Y. Acad. Sci. 1009:400-412(2003) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS33767.1. [Q9Y2I1-1]
CCDS63651.1. [Q9Y2I1-4]
CCDS63652.1. [Q9Y2I1-3]
PIRT17230.
RefSeqNP_001263222.1. NM_001276293.1.
NP_001263223.1. NM_001276294.1.
NP_009115.2. NM_007184.3.
UniGeneHs.435290.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3P0CX-ray2.27A/B18-124[»]
ProteinModelPortalQ9Y2I1.
SMRQ9Y2I1. Positions 18-123, 212-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116358. 6 interactions.
IntActQ9Y2I1. 4 interactions.
STRING9606.ENSP00000339958.

Chemistry

ChEMBLCHEMBL3923.

PTM databases

PhosphoSiteQ9Y2I1.

Polymorphism databases

DMDM296439287.

Proteomic databases

MaxQBQ9Y2I1.
PaxDbQ9Y2I1.
PRIDEQ9Y2I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345716; ENSP00000339958; ENSG00000010322. [Q9Y2I1-1]
ENST00000420808; ENSP00000392484; ENSG00000010322. [Q9Y2I1-4]
ENST00000479054; ENSP00000418232; ENSG00000010322. [Q9Y2I1-1]
GeneID11188.
KEGGhsa:11188.
UCSCuc003ded.4. human. [Q9Y2I1-1]
uc031sad.1. human. [Q9Y2I1-4]

Organism-specific databases

CTD11188.
GeneCardsGC03P052489.
HGNCHGNC:18006. NISCH.
HPAHPA023189.
MIM615507. gene.
neXtProtNX_Q9Y2I1.
PharmGKBPA31635.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269110.
HOVERGENHBG108189.
InParanoidQ9Y2I1.
OMAGNIEWAS.
OrthoDBEOG70ZZMH.
PhylomeDBQ9Y2I1.
TreeFamTF320547.

Enzyme and pathway databases

SignaLinkQ9Y2I1.

Gene expression databases

ArrayExpressQ9Y2I1.
BgeeQ9Y2I1.
CleanExHS_NISCH.
GenevestigatorQ9Y2I1.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR001611. Leu-rich_rpt.
IPR001683. Phox.
[Graphical view]
PfamPF13855. LRR_8. 1 hit.
PF00787. PX. 1 hit.
[Graphical view]
SMARTSM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF64268. SSF64268. 1 hit.
PROSITEPS51450. LRR. 6 hits.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNISCH. human.
GeneWikiNISCH.
GenomeRNAi11188.
NextBio42587.
PROQ9Y2I1.
SOURCESearch...

Entry information

Entry nameNISCH_HUMAN
AccessionPrimary (citable) accession number: Q9Y2I1
Secondary accession number(s): C9J245 expand/collapse secondary AC list , Q6PGP3, Q6PIB4, Q7L8M3, Q7Z2X6, Q9UES6, Q9UEU4, Q9UFW3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM