NISCH_HUMAN - dbPTM
NISCH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NISCH_HUMAN
UniProt AC Q9Y2I1
Protein Name Nischarin
Gene Name NISCH
Organism Homo sapiens (Human).
Sequence Length 1504
Subcellular Localization Cell membrane. Cytoplasm. Early endosome. Recycling endosome. 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 perin
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 (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..
Protein Sequence MATARTFGPEREAEPAKEARVVGSELVDTYTVYIIQVTDGSHEWTVKHRYSDFHDLHEKLVAERKIDKNLLPPKKIIGKNSRSLVEKREKDLEVYLQKLLAAFPGVTPRVLAHFLHFHFYEINGITAALAEELFEKGEQLLGAGEVFAIGPLQLYAVTEQLQQGKPTCASGDAKTDLGHILDFTCRLKYLKVSGTEGPFGTSNIQEQLLPFDLSIFKSLHQVEISHCDAKHIRGLVASKPTLATLSVRFSATSMKEVLVPEASEFDEWEPEGTTLEGPVTAVIPTWQALTTLDLSHNSVSEIDESVKLIPKIEFLDLSHNGLLVVDNLQHLYNLVHLDLSYNKLSSLEGLHTKLGNIKTLNLAGNLLESLSGLHKLYSLVNLDLRDNRIEQMEEVRSIGSLPCLEHVSLLNNPLSIIPDYRTKVLAQFGERASEVCLDDTVTTEKELDTVEVLKAIQKAKEVKSKLSNPEKKGGEDSRLSAAPCIRPSSSPPTVAPASASLPQPILSNQGIMFVQEEALASSLSSTDSLTPEHQPIAQGCSDSLESIPAGQAASDDLRDVPGAVGGASPEHAEPEVQVVPGSGQIIFLPFTCIGYTATNQDFIQRLSTLIRQAIERQLPAWIEAANQREEGQGEQGEEEDEEEEEEEDVAENRYFEMGPPDVEEEEGGGQGEEEEEEEEDEEAEEERLALEWALGADEDFLLEHIRILKVLWCFLIHVQGSIRQFAACLVLTDFGIAVFEIPHQESRGSSQHILSSLRFVFCFPHGDLTEFGFLMPELCLVLKVRHSENTLFIISDAANLHEFHADLRSCFAPQHMAMLCSPILYGSHTSLQEFLRQLLTFYKVAGGCQERSQGCFPVYLVYSDKRMVQTAAGDYSGNIEWASCTLCSAVRRSCCAPSEAVKSAAIPYWLLLTPQHLNVIKADFNPMPNRGTHNCRNRNSFKLSRVPLSTVLLDPTRSCTQPRGAFADGHVLELLVGYRFVTAIFVLPHEKFHFLRVYNQLRASLQDLKTVVIAKTPGTGGSPQGSFADGQPAERRASNDQRPQEVPAEALAPAPAEVPAPAPAAASASGPAKTPAPAEASTSALVPEETPVEAPAPPPAEAPAQYPSEHLIQATSEENQIPSHLPACPSLRHVASLRGSAIIELFHSSIAEVENEELRHLMWSSVVFYQTPGLEVTACVLLSTKAVYFVLHDGLRRYFSEPLQDFWHQKNTDYNNSPFHISQCFVLKLSDLQSVNVGLFDQHFRLTGSTPMQVVTCLTRDSYLTHCFLQHLMVVLSSLERTPSPEPVDKDFYSEFGNKTTGKMENYELIHSSRVKFTYPSEEEIGDLTFTVAQKMAEPEKAPALSILLYVQAFQVGMPPPGCCRGPLRPKTLLLTSSEIFLLDEDCVHYPLPEFAKEPPQRDRYRLDDGRRVRDLDRVLMGYQTYPQALTLVFDDVQGHDLMGSVTLDHFGEVPGGPARASQGREVQWQVFVPSAESREKLISLLARQWEALCGRELPVELTG
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
2Acetylation------MATARTFGP
------CCCCCCCCC		22.6719413330
50PhosphorylationEWTVKHRYSDFHDLH
EEEEEECCCCHHHHH		16.5929449344
51PhosphorylationWTVKHRYSDFHDLHE
EEEEECCCCHHHHHH		33.4827251275
54UbiquitinationKHRYSDFHDLHEKLV
EECCCCHHHHHHHHH		41.5322053931
59UbiquitinationDFHDLHEKLVAERKI
CHHHHHHHHHHHHCC		37.2029967540
79UbiquitinationPPKKIIGKNSRSLVE
CCHHHCCCCCHHHHH		41.1429967540
107PhosphorylationLAAFPGVTPRVLAHF
HHHCCCCCHHHHHHH		15.9928348404
214PhosphorylationQLLPFDLSIFKSLHQ
HHCCCCHHHHHHHCE		28.0224719451
244PhosphorylationASKPTLATLSVRFSA
CCCCEEEEEEEEECC		23.7621406692
246PhosphorylationKPTLATLSVRFSATS
CCEEEEEEEEECCCC		13.5920068231
250PhosphorylationATLSVRFSATSMKEV
EEEEEEECCCCCCEE		21.77-
252PhosphorylationLSVRFSATSMKEVLV
EEEEECCCCCCEEEC		28.31-
337UbiquitinationHLYNLVHLDLSYNKL
HHHHHHHHCCCHHHH		5.7422053931
353UbiquitinationSLEGLHTKLGNIKTL
CCCCHHHHCCCHHHE		43.5832015554
358UbiquitinationHTKLGNIKTLNLAGN
HHHCCCHHHEHHHHH		51.4629967540
396UbiquitinationIEQMEEVRSIGSLPC
HHHHHHHHCCCCCCH		26.3221963094
433PhosphorylationAQFGERASEVCLDDT
HHHHHHHHHCCCCCC		36.4623312004
440PhosphorylationSEVCLDDTVTTEKEL
HHCCCCCCCCCHHHH		21.3023312004
442PhosphorylationVCLDDTVTTEKELDT
CCCCCCCCCHHHHHH		31.1823312004
443PhosphorylationCLDDTVTTEKELDTV
CCCCCCCCHHHHHHH		40.5023312004
445UbiquitinationDDTVTTEKELDTVEV
CCCCCCHHHHHHHHH		62.5822053931
449PhosphorylationTTEKELDTVEVLKAI
CCHHHHHHHHHHHHH		31.0623312004
452UbiquitinationKELDTVEVLKAIQKA
HHHHHHHHHHHHHHH		6.0522053931
454UbiquitinationLDTVEVLKAIQKAKE
HHHHHHHHHHHHHHH		48.9332015554
464PhosphorylationQKAKEVKSKLSNPEK
HHHHHHHHHHCCCHH		43.9627251275
467PhosphorylationKEVKSKLSNPEKKGG
HHHHHHHCCCHHCCC		54.8227251275
4712-HydroxyisobutyrylationSKLSNPEKKGGEDSR
HHHCCCHHCCCCCCC		58.96-
477PhosphorylationEKKGGEDSRLSAAPC
HHCCCCCCCCCCCCC		30.7120068231
480 (in isoform 4)Phosphorylation-22.6722210691
488PhosphorylationAAPCIRPSSSPPTVA
CCCCCCCCCCCCCCC		33.3327251275
488 (in isoform 3)Phosphorylation-33.3328348404
488 (in isoform 4)Phosphorylation-33.3326552605
489 (in isoform 3)Phosphorylation-49.9328348404
489 (in isoform 4)Phosphorylation-49.9326552605
490PhosphorylationPCIRPSSSPPTVAPA
CCCCCCCCCCCCCCC		38.9629116813
490 (in isoform 3)Phosphorylation-38.9628348404
490 (in isoform 4)Phosphorylation-38.9626552605
493PhosphorylationRPSSSPPTVAPASAS
CCCCCCCCCCCCCCC		32.4629116813
493 (in isoform 3)Phosphorylation-32.4628348404
493 (in isoform 4)Phosphorylation-32.4626552605
498 (in isoform 3)Phosphorylation-19.8224043423
498 (in isoform 4)Phosphorylation-19.8227251275
498 (in isoform 2)Ubiquitination-19.8221890473
500 (in isoform 3)Phosphorylation-37.7824043423
500 (in isoform 4)Phosphorylation-37.7827251275
503UbiquitinationPASASLPQPILSNQG
CCCCCCCCCCCCCCC		42.8521890473
504 (in isoform 2)Ubiquitination-27.7821890473
507 (in isoform 3)Phosphorylation-28.0324043423
507 (in isoform 4)Phosphorylation-28.0327251275
509UbiquitinationPQPILSNQGIMFVQE
CCCCCCCCCEEEECH		39.1422817900
511UbiquitinationPILSNQGIMFVQEEA
CCCCCCCEEEECHHH		1.0821963094
541PhosphorylationQPIAQGCSDSLESIP
CCCCCCCCCCHHCCC		36.74-
543PhosphorylationIAQGCSDSLESIPAG
CCCCCCCCHHCCCCC		20.10-
546PhosphorylationGCSDSLESIPAGQAA
CCCCCHHCCCCCCCC		38.8826074081
554PhosphorylationIPAGQAASDDLRDVP
CCCCCCCCCCCCCCC		34.3726074081
568PhosphorylationPGAVGGASPEHAEPE
CCCCCCCCHHHCCCC		33.8126074081
618UbiquitinationRQAIERQLPAWIEAA
HHHHHHHHHHHHHHH		3.8121890473
624UbiquitinationQLPAWIEAANQREEG
HHHHHHHHHHHCCCC		11.5422817900
654PhosphorylationEDVAENRYFEMGPPD
HHHHHHCCCCCCCCC		18.5728796482
755PhosphorylationGSSQHILSSLRFVFC
CCHHHHHHHCEEEEE		27.0717081983
756PhosphorylationSSQHILSSLRFVFCF
CHHHHHHHCEEEEEE		21.8125954137
779 (in isoform 2)Ubiquitination-2.0521890473
784UbiquitinationELCLVLKVRHSENTL
HHHEEEEEECCCCEE		6.1021890473
788 (in isoform 2)Ubiquitination-48.3821890473
792 (in isoform 2)Ubiquitination-4.3621890473
793UbiquitinationHSENTLFIISDAANL
CCCCEEEEEECCCCH		3.1122817900
797UbiquitinationTLFIISDAANLHEFH
EEEEEECCCCHHHHH		7.4621890473
805 (in isoform 2)Ubiquitination-23.89-
810UbiquitinationFHADLRSCFAPQHMA
HHHHHHHCCCHHHHH		2.4523503661
843UbiquitinationRQLLTFYKVAGGCQE
HHHHHHHHHHCCCHH		22.7822053931
865UbiquitinationVYLVYSDKRMVQTAA
EEEEEECCCEEECCC		36.13-
883PhosphorylationSGNIEWASCTLCSAV
CCCEEEHHHHHHHHH		14.54-
899UbiquitinationRSCCAPSEAVKSAAI
HHCCCCHHHHHHCHH		57.3221890473
902UbiquitinationCAPSEAVKSAAIPYW
CCCHHHHHHCHHCHH		41.2321963094
908UbiquitinationVKSAAIPYWLLLTPQ
HHHCHHCHHHHHCHH		11.5422817900
912UbiquitinationAIPYWLLLTPQHLNV
HHCHHHHHCHHHHCE		6.5121890473
925UbiquitinationNVIKADFNPMPNRGT
CEEECCCCCCCCCCC		32.2923503661
942UbiquitinationCRNRNSFKLSRVPLS
CCCCCCCCCCCCCCC		45.43-
1004PhosphorylationVYNQLRASLQDLKTV
HHHHHHHHHHHCCEE		21.8227251275
1009UbiquitinationRASLQDLKTVVIAKT
HHHHHHCCEEEEEEC		47.7921906983
1009 (in isoform 1)Ubiquitination-47.7921890473
1015AcetylationLKTVVIAKTPGTGGS
CCEEEEEECCCCCCC		44.0919657421
1015UbiquitinationLKTVVIAKTPGTGGS
CCEEEEEECCCCCCC		44.0921906983
1015 (in isoform 1)Ubiquitination-44.0921890473
1016PhosphorylationKTVVIAKTPGTGGSP
CEEEEEECCCCCCCC		20.2327251275
1019PhosphorylationVIAKTPGTGGSPQGS
EEEECCCCCCCCCCC		39.3025262027
1022PhosphorylationKTPGTGGSPQGSFAD
ECCCCCCCCCCCCCC		18.5225159151
1026PhosphorylationTGGSPQGSFADGQPA
CCCCCCCCCCCCCCC		16.4126074081
1038PhosphorylationQPAERRASNDQRPQE
CCCCCCCCCCCCCCC		38.8428464451
1067PhosphorylationAPAPAAASASGPAKT
CCCCCHHHCCCCCCC		20.4526074081
1069PhosphorylationAPAAASASGPAKTPA
CCCHHHCCCCCCCCC		42.7026074081
1183PhosphorylationVTACVLLSTKAVYFV
HHEEHHHCCCHHHEE		24.5724719451
1200PhosphorylationDGLRRYFSEPLQDFW
HHHHHHHCCCHHHHH		29.3928857561
1277PhosphorylationQHLMVVLSSLERTPS
HHHHHHHHHHCCCCC		22.6724719451
1278PhosphorylationHLMVVLSSLERTPSP
HHHHHHHHHCCCCCC		30.0426074081
1282PhosphorylationVLSSLERTPSPEPVD
HHHHHCCCCCCCCCC		20.8128102081
1284PhosphorylationSSLERTPSPEPVDKD
HHHCCCCCCCCCCHH		41.0823401153
1290UbiquitinationPSPEPVDKDFYSEFG
CCCCCCCHHHHHHHC		50.3922817900
1290 (in isoform 1)Ubiquitination-50.3921890473
1293PhosphorylationEPVDKDFYSEFGNKT
CCCCHHHHHHHCCCC		19.8825884760
1294PhosphorylationPVDKDFYSEFGNKTT
CCCHHHHHHHCCCCC		26.8328796482
1299UbiquitinationFYSEFGNKTTGKMEN
HHHHHCCCCCCCEEC		48.0921906983
1299 (in isoform 1)Ubiquitination-48.0921890473
1303UbiquitinationFGNKTTGKMENYELI
HCCCCCCCEECCEEE		40.7322817900
1303AcetylationFGNKTTGKMENYELI
HCCCCCCCEECCEEE		40.7325953088
1303 (in isoform 1)Ubiquitination-40.7321890473
1307PhosphorylationTTGKMENYELIHSSR
CCCCEECCEEEECCC		9.9828796482
1312PhosphorylationENYELIHSSRVKFTY
ECCEEEECCCEEEEC		16.9129083192
1313PhosphorylationNYELIHSSRVKFTYP
CCEEEECCCEEEECC		27.2529083192
1316UbiquitinationLIHSSRVKFTYPSEE
EEECCCEEEECCCHH		30.7723503661
1335UbiquitinationLTFTVAQKMAEPEKA
EEEEEHHHHCCCCCC		30.2729967540
1372PhosphorylationRGPLRPKTLLLTSSE
CCCCCCCEEEEECCE		25.8924719451
1376PhosphorylationRPKTLLLTSSEIFLL
CCCEEEEECCEEEEE		30.1224719451
1481UbiquitinationPSAESREKLISLLAR
CCHHHHHHHHHHHHH		50.43-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NISCH_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IRS1_HUMANIRS1physical
11912194
IRS2_HUMANIRS2physical
11912194
K1671_HUMANKIAA1671physical
27173435
P85A_HUMANPIK3R1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00697Tizanidine
Regulatory Network of NISCH_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-1022, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1284, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-1022, AND MASS SPECTROMETRY.

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