NISCH_MOUSE - dbPTM
NISCH_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NISCH_MOUSE
UniProt AC Q80TM9
Protein Name Nischarin
Gene Name Nisch
Organism Mus musculus (Mouse).
Sequence Length 1593
Subcellular Localization Cell membrane. Cytoplasm . Early endosome. Recycling endosome. Enriched in the early/sorting and recycling endosomes (By similarity). Colocalized in early/sorting endosomes with EEA1 and SNX2 and in recycling endosomes with transferrin receptor (By s
Protein Description 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)..
Protein Sequence MAAATLSFGPEREAEPAKEARVVGSELVDTYTVYVIQVTDGNHEWTIKHRYSDFHDLHEKLVAERKIDKSLLPPKKIIGKNSRSLVEKRERDLEVYLQTLLTTFPDVAPRVLAHFLHFHLYEVNGVTAALAEELFEKGEQLLGAGEVFAIRPLQLYAITEQLQQGKPTCASGDAKTDLGHILDFTCRLKYLKVSGTEGPFGTSNIKEQLLPFDLSIFKSLHQVEISHCDAKHIRGLVTSKPTLATMSVRFSATSMKEVLAPEASEFDEWEPEGTATLGGPVTAIIPTWQALTTLDLSHNSICEIDESVKLIPKIEYLDLSHNGLRVVDNLQHLYNLVHLDLSYNKLSSLEGVHTKLGNVKTLNLAGNFLESLSGLHKLYSLVNVDLRDNRIEQLDEVKSIGSLPCLERLTLLNNPLSIIPDYRTKVLSQFGERASEICLDDVATTEKELDTVEVLKAIQKAKDVKSKLSNTEKKAGEDFRLPPAPCIRPGGSPPAAPASASLPQPILSNQGIMFVQEEALASSLSSTDSLPPEDHRPIARACSDSLESIPAGQVASDDLRDVPGAVGGVSPDHAEPEVQVVPGSGQIIFLPFTCIGYTATNQDFIQRLSTLIRQAIERQLPAWIEAANQREEAHGEQGEEEEEEEEEEDVAENRYFEMGPPDAEEEEGSGQGEEDEEDEDEEAEEERLALEWALGADEDFLLEHIRILKVLWCFLIHVQGSIRQFAACLVLTDFGIAVFEIPHQESRGSSQHILSSLRFVFCFPHGDLTEFGFLMPELCLVLKVRHSENTLFIISDAANLHEFHADLRSCFAPQHMAMLCSPILYGSHTTLQEFLRQLLTFYKVAGGSQERSQGCFPVYLVYSDKRMVQTPAGDYSGNIEWASCTLCSAVRRSCCAPSEAVKSAAIPYWLLLTSQHLNVIKADFNPMPNRGTHNCRNRNSFKLSRVPLSTVLLDPTRSCTQPRGAFADGHVLELLVGYRFVTAIFVLPHEKFHFLRVYNQLRASLQDLKTVVISKNPSAKPRNQPAKSRASAEQRLQETPADAPAPAAVPPTASAPAPAEALAPDLAPVQAPGEDRGLTSAEAPAAAEAPAAAEAPAAAEAPAAAEAPAAAEAPAAAEAPAPAEAPAAAEAPAAAEAPAAAEAPAAAEAPASAEAPAPNQAPAPARGPAPARGPAPAGGPAPAEALAQAEVPAQYPSERLIQSTSEENQIPSHLPVCPSLQHIARLRGRAIIDLFHNSIAEVENEELRHLLWSSVVFYQTPGLEVTACVLLSSKAVYFILHDGLRRYFSEPLQDFWHQKNTDYNNSPFHVSQCFVLKLSDLQSVNVGLFDQYFRLTGSSPTQVVTCLTRDSYLTHCFLQHLMLVLSSLERTPSPEPVDKDFYSEFGDKNTGKMENYELIHSSRVKFTYPSEEEVGDLTYIVAQKMADPAKNPALSILLYIQAFQVVTPHLGRGRGPLRPKTLLLTSAEIFLLDEDYIHYPLPEFAKEPPQRDRYRLDDGRRVRDLDRVLMGYYPYPQALTLVFDDTQGHDLMGSVTLDHFGEMPGGPGRVGQGREVQWQVFVPSAESREKLISLLARQWEALCGRELPVELTG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
5Phosphorylation---MAAATLSFGPER
---CCCCCCCCCCHH
20.4328066266
7Phosphorylation-MAAATLSFGPEREA
-CCCCCCCCCCHHCC
24.6526824392
52PhosphorylationWTIKHRYSDFHDLHE
EEEEEECCCHHHHHH
33.4829899451
190PhosphorylationDFTCRLKYLKVSGTE
HHEEEEEEEEECCCC
19.1520116462
206UbiquitinationPFGTSNIKEQLLPFD
CCCCCCHHHHHCCCC
43.59-
238PhosphorylationKHIRGLVTSKPTLAT
HHHHCCCCCCCCEEE
35.7526643407
239PhosphorylationHIRGLVTSKPTLATM
HHHCCCCCCCCEEEE
29.2026643407
242PhosphorylationGLVTSKPTLATMSVR
CCCCCCCCEEEEEEE
32.5328576409
247PhosphorylationKPTLATMSVRFSATS
CCCEEEEEEEECCCC
13.04-
251PhosphorylationATMSVRFSATSMKEV
EEEEEEECCCCHHHH
21.77-
253PhosphorylationMSVRFSATSMKEVLA
EEEEECCCCHHHHHC
28.31-
254PhosphorylationSVRFSATSMKEVLAP
EEEECCCCHHHHHCC
27.81-
264PhosphorylationEVLAPEASEFDEWEP
HHHCCCCCCCCCCCC
36.81-
360UbiquitinationHTKLGNVKTLNLAGN
HHHCCCCEEEECCHH
51.82-
425UbiquitinationIIPDYRTKVLSQFGE
CCCCHHHHHHHHHHH
31.9822790023
436PhosphorylationQFGERASEICLDDVA
HHHHHHHHHCHHCCC
36.4219144319
447UbiquitinationDDVATTEKELDTVEV
HCCCCCHHHCHHHHH
62.58-
492 (in isoform 6)Phosphorylation-33.3625521595
492PhosphorylationPCIRPGGSPPAAPAS
CCCCCCCCCCCCCCC
33.3626824392
499 (in isoform 6)Phosphorylation-19.8222324799
501 (in isoform 6)Phosphorylation-37.7822324799
543PhosphorylationRPIARACSDSLESIP
HHHHHHHHHCHHCCC
29.2925521595
545PhosphorylationIARACSDSLESIPAG
HHHHHHHCHHCCCCC
20.1025521595
548PhosphorylationACSDSLESIPAGQVA
HHHHCHHCCCCCCCC
38.8825521595
556PhosphorylationIPAGQVASDDLRDVP
CCCCCCCCCCCCCCC
32.5725619855
669PhosphorylationDAEEEEGSGQGEEDE
CCCCCCCCCCCCCCC
31.0927180971
721PhosphorylationFLIHVQGSIRQFAAC
HHHHHHCHHHHHHHH
9.4826824392
755PhosphorylationGSSQHILSSLRFVFC
CCHHHHHHHCEEEEE
27.0725159016
756PhosphorylationSSQHILSSLRFVFCF
CHHHHHHHCEEEEEE
21.8125159016
843UbiquitinationRQLLTFYKVAGGSQE
HHHHHHHHHHCCCCH
22.78-
865UbiquitinationVYLVYSDKRMVQTPA
EEEEEECCCEEECCC
36.1322790023
870PhosphorylationSDKRMVQTPAGDYSG
ECCCEEECCCCCCCC
12.0527600695
902UbiquitinationCAPSEAVKSAAIPYW
CCCHHHHHHCHHHHH
41.23-
991UbiquitinationIFVLPHEKFHFLRVY
EEEECCCHHHHHHHH
40.90-
1009UbiquitinationRASLQDLKTVVISKN
HHHHHHCCEEEEECC
47.7922790023
1367PhosphorylationHLMLVLSSLERTPSP
HHHHHHHHHCCCCCC
30.0424704852
1371PhosphorylationVLSSLERTPSPEPVD
HHHHHCCCCCCCCCC
20.8127742792
1373PhosphorylationSSLERTPSPEPVDKD
HHHCCCCCCCCCCHH
41.0825521595
1379UbiquitinationPSPEPVDKDFYSEFG
CCCCCCCHHHHHHHC
50.3922790023
1382PhosphorylationEPVDKDFYSEFGDKN
CCCCHHHHHHHCCCC
19.8827742792
1383PhosphorylationPVDKDFYSEFGDKNT
CCCHHHHHHHCCCCC
26.8325159016
1388UbiquitinationFYSEFGDKNTGKMEN
HHHHHCCCCCCCCCC
57.7122790023
1392UbiquitinationFGDKNTGKMENYELI
HCCCCCCCCCCEEEE
40.7922790023
1396PhosphorylationNTGKMENYELIHSSR
CCCCCCCEEEEEECC
9.9825159016
1405UbiquitinationLIHSSRVKFTYPSEE
EEEECCEEEECCCHH
30.7722790023
1570UbiquitinationPSAESREKLISLLAR
CCHHHHHHHHHHHHH
50.4322790023

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of NISCH_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NISCH_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of NISCH_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NISCH_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NISCH_MOUSE

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Related Literatures of Post-Translational Modification

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