NF2IP_HUMAN - dbPTM
NF2IP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NF2IP_HUMAN
UniProt AC Q8NCF5
Protein Name NFATC2-interacting protein
Gene Name NFATC2IP
Organism Homo sapiens (Human).
Sequence Length 419
Subcellular Localization Nucleus. Cytoplasm. TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm and prevents its translocation to the nucleus..
Protein Description In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression (By similarity). Down-regulates formation of poly-SUMO chains by UBE2I/UBC9 (By similarity)..
Protein Sequence MAEPVGKRGRWSGGSGAGRGGRGGWGGRGRRPRAQRSPSRGTLDVVSVDLVTDSDEEILEVATARGAADEVEVEPPEPPGPVASRDNSNSDSEGEDRRPAGPPREPVRRRRRLVLDPGEAPLVPVYSGKVKSSLRLIPDDLSLLKLYPPGDEEEAELADSSGLYHEGSPSPGSPWKTKLRTKDKEEKKKTEFLDLDNSPLSPPSPRTKSRTHTRALKKLSEVNKRLQDLRSCLSPKPPQGQEQQGQEDEVVLVEGPTLPETPRLFPLKIRCRADLVRLPLRMSEPLQSVVDHMATHLGVSPSRILLLFGETELSPTATPRTLKLGVADIIDCVVLTSSPEATETSQQLQLRVQGKEKHQTLEVSLSRDSPLKTLMSHYEEAMGLSGRKLSFFFDGTKLSGRELPADLGMESGDLIEVWG
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
12PhosphorylationVGKRGRWSGGSGAGR
CCCCCCCCCCCCCCC		31.7328258704
15PhosphorylationRGRWSGGSGAGRGGR
CCCCCCCCCCCCCCC		29.0628258704
37PhosphorylationRRPRAQRSPSRGTLD
CCCCCCCCCCCCCEE		18.3627422710
42PhosphorylationQRSPSRGTLDVVSVD
CCCCCCCCEEEEEEE		20.7620873877
47PhosphorylationRGTLDVVSVDLVTDS
CCCEEEEEEEECCCC		15.1221406692
52PhosphorylationVVSVDLVTDSDEEIL
EEEEEECCCCCHHHH		36.7620873877
54PhosphorylationSVDLVTDSDEEILEV
EEEECCCCCHHHHHH		37.2427422710
63PhosphorylationEEILEVATARGAADE
HHHHHHHHHCCCCCE		23.2821406692
84PhosphorylationEPPGPVASRDNSNSD
CCCCCCCCCCCCCCC		40.1623401153
88PhosphorylationPVASRDNSNSDSEGE
CCCCCCCCCCCCCCC		41.8420164059
90PhosphorylationASRDNSNSDSEGEDR
CCCCCCCCCCCCCCC		42.1929255136
92PhosphorylationRDNSNSDSEGEDRRP
CCCCCCCCCCCCCCC		47.5229255136
126PhosphorylationEAPLVPVYSGKVKSS
CCCCEEECCCCCCCC		12.9725850435
127PhosphorylationAPLVPVYSGKVKSSL
CCCEEECCCCCCCCE		32.1621712546
129SumoylationLVPVYSGKVKSSLRL
CEEECCCCCCCCEEE		40.32-
129SumoylationLVPVYSGKVKSSLRL
CEEECCCCCCCCEEE		40.3228112733
129UbiquitinationLVPVYSGKVKSSLRL
CEEECCCCCCCCEEE		40.3221906983
129 (in isoform 1)Ubiquitination-40.3221890473
129AcetylationLVPVYSGKVKSSLRL
CEEECCCCCCCCEEE		40.3225953088
131SumoylationPVYSGKVKSSLRLIP
EECCCCCCCCEEECC		37.5028112733
131UbiquitinationPVYSGKVKSSLRLIP
EECCCCCCCCEEECC		37.5022817900
142PhosphorylationRLIPDDLSLLKLYPP
EECCCCCHHHCCCCC		38.3521815630
145UbiquitinationPDDLSLLKLYPPGDE
CCCCHHHCCCCCCCH		51.7929967540
147PhosphorylationDLSLLKLYPPGDEEE
CCHHHCCCCCCCHHH		13.0422199227
160PhosphorylationEEAELADSSGLYHEG
HHHHHHHCCCCCCCC		22.2423663014
161PhosphorylationEAELADSSGLYHEGS
HHHHHHCCCCCCCCC		33.1123663014
164PhosphorylationLADSSGLYHEGSPSP
HHHCCCCCCCCCCCC		11.0125159151
168PhosphorylationSGLYHEGSPSPGSPW
CCCCCCCCCCCCCCC		21.1525159151
170PhosphorylationLYHEGSPSPGSPWKT
CCCCCCCCCCCCCCC		43.5225159151
173PhosphorylationEGSPSPGSPWKTKLR
CCCCCCCCCCCCCCC		30.8525159151
176UbiquitinationPSPGSPWKTKLRTKD
CCCCCCCCCCCCCCC		38.8829967540
190PhosphorylationDKEEKKKTEFLDLDN
CHHHHHHCCCCCCCC		40.6323927012
198PhosphorylationEFLDLDNSPLSPPSP
CCCCCCCCCCCCCCC		27.2123927012
201PhosphorylationDLDNSPLSPPSPRTK
CCCCCCCCCCCCCCC		37.8429255136
204PhosphorylationNSPLSPPSPRTKSRT
CCCCCCCCCCCCCHH		30.3319664994
207PhosphorylationLSPPSPRTKSRTHTR
CCCCCCCCCCHHHHH		36.4329514088
208AcetylationSPPSPRTKSRTHTRA
CCCCCCCCCHHHHHH		38.9411794033
209PhosphorylationPPSPRTKSRTHTRAL
CCCCCCCCHHHHHHH		41.6228111955
218UbiquitinationTHTRALKKLSEVNKR
HHHHHHHHHHHHHHH		59.0824816145
218MethylationTHTRALKKLSEVNKR
HHHHHHHHHHHHHHH		59.08110869219
218SumoylationTHTRALKKLSEVNKR
HHHHHHHHHHHHHHH		59.08-
218SumoylationTHTRALKKLSEVNKR
HHHHHHHHHHHHHHH		59.08-
220PhosphorylationTRALKKLSEVNKRLQ
HHHHHHHHHHHHHHH		48.6729496963
224UbiquitinationKKLSEVNKRLQDLRS
HHHHHHHHHHHHHHH		60.7130230243
231PhosphorylationKRLQDLRSCLSPKPP
HHHHHHHHHHCCCCC		27.0623401153
234PhosphorylationQDLRSCLSPKPPQGQ
HHHHHHHCCCCCCCC		34.8930278072
234O-linked_GlycosylationQDLRSCLSPKPPQGQ
HHHHHHHCCCCCCCC		34.89OGP
257PhosphorylationVVLVEGPTLPETPRL
EEEEECCCCCCCCCC		66.8426074081
261PhosphorylationEGPTLPETPRLFPLK
ECCCCCCCCCCCCCE		16.2726552605
268UbiquitinationTPRLFPLKIRCRADL
CCCCCCCEEEECCEE		28.4822817900
268 (in isoform 1)Ubiquitination-28.4821890473
268AcetylationTPRLFPLKIRCRADL
CCCCCCCEEEECCEE		28.4825953088
283PhosphorylationVRLPLRMSEPLQSVV
EECCCCCCCCHHHHH		29.6324043423
288PhosphorylationRMSEPLQSVVDHMAT
CCCCCHHHHHHHHHH		31.6130108239
295PhosphorylationSVVDHMATHLGVSPS
HHHHHHHHHCCCCHH		15.2830108239
300PhosphorylationMATHLGVSPSRILLL
HHHHCCCCHHHEEEE		18.5022617229
302PhosphorylationTHLGVSPSRILLLFG
HHCCCCHHHEEEEEC		25.1728464451
311PhosphorylationILLLFGETELSPTAT
EEEEECCCCCCCCCC		42.4829255136
314PhosphorylationLFGETELSPTATPRT
EECCCCCCCCCCCCC		17.6129255136
316PhosphorylationGETELSPTATPRTLK
CCCCCCCCCCCCCCC		39.5229255136
318PhosphorylationTELSPTATPRTLKLG
CCCCCCCCCCCCCCC		18.7821712546
336PhosphorylationIIDCVVLTSSPEATE
EEEEEEEECCCCCCH		18.6230278072
337O-linked_GlycosylationIDCVVLTSSPEATET
EEEEEEECCCCCCHH		39.4723301498
337PhosphorylationIDCVVLTSSPEATET
EEEEEEECCCCCCHH		39.4730278072
338PhosphorylationDCVVLTSSPEATETS
EEEEEECCCCCCHHH		22.8630278072
342PhosphorylationLTSSPEATETSQQLQ
EECCCCCCHHHHHHH		37.8330278072
344PhosphorylationSSPEATETSQQLQLR
CCCCCCHHHHHHHHH		27.7323663014
345PhosphorylationSPEATETSQQLQLRV
CCCCCHHHHHHHHHH		15.0823663014
357SumoylationLRVQGKEKHQTLEVS
HHHCCCCCCEEEEEE		44.49-
357SumoylationLRVQGKEKHQTLEVS
HHHCCCCCCEEEEEE		44.49-
360PhosphorylationQGKEKHQTLEVSLSR
CCCCCCEEEEEEECC		25.3023927012
364PhosphorylationKHQTLEVSLSRDSPL
CCEEEEEEECCCCHH		15.9723927012
366PhosphorylationQTLEVSLSRDSPLKT
EEEEEEECCCCHHHH		26.9129255136
369PhosphorylationEVSLSRDSPLKTLMS
EEEECCCCHHHHHHH		30.9029255136
373PhosphorylationSRDSPLKTLMSHYEE
CCCCHHHHHHHHHHH		35.0626074081
376PhosphorylationSPLKTLMSHYEEAMG
CHHHHHHHHHHHHHC		26.4826074081
378PhosphorylationLKTLMSHYEEAMGLS
HHHHHHHHHHHHCCC		14.2528787133
385PhosphorylationYEEAMGLSGRKLSFF
HHHHHCCCCCEEEEE		30.7228555341
388UbiquitinationAMGLSGRKLSFFFDG
HHCCCCCEEEEEECC		52.59-
388SumoylationAMGLSGRKLSFFFDG
HHCCCCCEEEEEECC		52.59-
388SumoylationAMGLSGRKLSFFFDG
HHCCCCCEEEEEECC		52.59-
390PhosphorylationGLSGRKLSFFFDGTK
CCCCCEEEEEECCCC		24.0425159151
396PhosphorylationLSFFFDGTKLSGREL
EEEEECCCCCCCCCC		30.5623186163
397SumoylationSFFFDGTKLSGRELP
EEEECCCCCCCCCCC		46.30-
397SumoylationSFFFDGTKLSGRELP
EEEECCCCCCCCCCC		46.30-
397UbiquitinationSFFFDGTKLSGRELP
EEEECCCCCCCCCCC		46.3033845483
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 NF2IP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NF2IP_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 NF2IP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD8_HUMANCHD8physical
28514442
ARP6_HUMANACTR6physical
28514442
ELF2_HUMANELF2physical
28514442
ZNHI1_HUMANZNHIT1physical
28514442
PDLI5_HUMANPDLIM5physical
28514442
SRCAP_HUMANSRCAPphysical
28514442
VPS72_HUMANVPS72physical
28514442
RHEB_HUMANRHEBphysical
28514442
DMAP1_HUMANDMAP1physical
28514442
PDLI7_HUMANPDLIM7physical
28514442
IF4G3_HUMANEIF4G3physical
28514442
IF4G1_HUMANEIF4G1physical
28514442
SMCA1_HUMANSMARCA1physical
28514442
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
There are no disease associations of PTM sites.
Regulatory Network of NF2IP_HUMAN

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Related Literatures of Post-Translational Modification
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-204, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-198; SER-201;SER-204 AND SER-390, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-90; SER-92 ANDSER-204, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, AND MASSSPECTROMETRY.

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