NAB2_HUMAN - dbPTM
NAB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAB2_HUMAN
UniProt AC Q15742
Protein Name NGFI-A-binding protein 2
Gene Name NAB2
Organism Homo sapiens (Human).
Sequence Length 525
Subcellular Localization Nucleus. Isoform 2 is not localized to the nucleus..
Protein Description Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability (By similarity)..
Protein Sequence MHRAPSPTAEQPPGGGDSARRTLQPRLKPSARAMALPRTLGELQLYRVLQRANLLSYYETFIQQGGDDVQQLCEAGEEEFLEIMALVGMATKPLHVRRLQKALREWATNPGLFSQPVPAVPVSSIPLFKISETAGTRKGSMSNGHGSPGEKAGSARSFSPKSPLELGEKLSPLPGGPGAGDPRIWPGRSTPESDVGAGGEEEAGSPPFSPPAGGGVPEGTGAGGLAAGGTGGGPDRLEPEMVRMVVESVERIFRSFPRGDAGEVTSLLKLNKKLARSVGHIFEMDDNDSQKEEEIRKYSIIYGRFDSKRREGKQLSLHELTINEAAAQFCMRDNTLLLRRVELFSLSRQVARESTYLSSLKGSRLHPEELGGPPLKKLKQEVGEQSHPEIQQPPPGPESYVPPYRPSLEEDSASLSGESLDGHLQAVGSCPRLTPPPADLPLALPAHGLWSRHILQQTLMDEGLRLARLVSHDRVGRLSPCVPAKPPLAEFEEGLLDRCPAPGPHPALVEGRRSSVKVEAEASRQ
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
6Phosphorylation--MHRAPSPTAEQPP
--CCCCCCCCCCCCC		33.6219664994
8PhosphorylationMHRAPSPTAEQPPGG
CCCCCCCCCCCCCCC		47.3530266825
18PhosphorylationQPPGGGDSARRTLQP
CCCCCCCHHHHHCCC		27.2723090842
123O-linked_GlycosylationPVPAVPVSSIPLFKI
CCCCCCCCCCCEEEE		19.2429351928
131PhosphorylationSIPLFKISETAGTRK
CCCEEEEECCCCCCC		29.5027251275
140PhosphorylationTAGTRKGSMSNGHGS
CCCCCCCCCCCCCCC		23.2829396449
142PhosphorylationGTRKGSMSNGHGSPG
CCCCCCCCCCCCCCC		41.1630576142
147PhosphorylationSMSNGHGSPGEKAGS
CCCCCCCCCCCCCCC		24.8525849741
154PhosphorylationSPGEKAGSARSFSPK
CCCCCCCCCCCCCCC		25.9322210691
157PhosphorylationEKAGSARSFSPKSPL
CCCCCCCCCCCCCCC		29.7723927012
159PhosphorylationAGSARSFSPKSPLEL
CCCCCCCCCCCCCHH		32.4423927012
162PhosphorylationARSFSPKSPLELGEK
CCCCCCCCCCHHCCC		37.7929255136
169UbiquitinationSPLELGEKLSPLPGG
CCCHHCCCCCCCCCC		53.0929967540
169SumoylationSPLELGEKLSPLPGG
CCCHHCCCCCCCCCC		53.09-
171PhosphorylationLELGEKLSPLPGGPG
CHHCCCCCCCCCCCC		35.1429255136
189PhosphorylationPRIWPGRSTPESDVG
CCCCCCCCCCHHHCC		54.9825850435
190PhosphorylationRIWPGRSTPESDVGA
CCCCCCCCCHHHCCC		29.7025850435
193PhosphorylationPGRSTPESDVGAGGE
CCCCCCHHHCCCCCC		38.5125850435
205PhosphorylationGGEEEAGSPPFSPPA
CCCCCCCCCCCCCCC		36.1329496963
209PhosphorylationEAGSPPFSPPAGGGV
CCCCCCCCCCCCCCC		35.4325850435
220PhosphorylationGGGVPEGTGAGGLAA
CCCCCCCCCCCCCCC		23.3825850435
230PhosphorylationGGLAAGGTGGGPDRL
CCCCCCCCCCCCCCC		31.5625850435
266PhosphorylationGDAGEVTSLLKLNKK
CCHHHHHHHHHHHHH		36.5624719451
269UbiquitinationGEVTSLLKLNKKLAR
HHHHHHHHHHHHHHH		56.1429967540
277PhosphorylationLNKKLARSVGHIFEM
HHHHHHHHHCCCEEC		27.1823401153
289PhosphorylationFEMDDNDSQKEEEIR
EECCCCCHHHHHHHH		49.7829507054
316PhosphorylationRREGKQLSLHELTIN
CCCCCCCEEEEEEHH		25.7824043423
321PhosphorylationQLSLHELTINEAAAQ
CCEEEEEEHHHHHHH		20.8324043423
358PhosphorylationARESTYLSSLKGSRL
HHHHHHHHCCCCCCC		24.1824719451
361UbiquitinationSTYLSSLKGSRLHPE
HHHHHCCCCCCCCHH		57.7127667366
361SumoylationSTYLSSLKGSRLHPE
HHHHHCCCCCCCCHH		57.71-
361SumoylationSTYLSSLKGSRLHPE
HHHHHCCCCCCCCHH		57.71-
376UbiquitinationELGGPPLKKLKQEVG
HHCCCCHHHHHHHHH		62.9329967540
376AcetylationELGGPPLKKLKQEVG
HHCCCCHHHHHHHHH		62.9330590651
379SumoylationGPPLKKLKQEVGEQS
CCCHHHHHHHHHHCC		53.9821836637
407 (in isoform 3)Phosphorylation-39.1427732954
412 (in isoform 3)Phosphorylation-24.0427732954
414 (in isoform 3)Phosphorylation-27.3327732954
416 (in isoform 3)Phosphorylation-37.7127732954
419 (in isoform 3)Phosphorylation-34.9727732954
434PhosphorylationVGSCPRLTPPPADLP
CCCCCCCCCCCCCCC		34.7230266825
471PhosphorylationLRLARLVSHDRVGRL
HHHHHHHHCCCCCCC		25.0224719451
479PhosphorylationHDRVGRLSPCVPAKP
CCCCCCCCCCCCCCC		18.2029255136
514PhosphorylationALVEGRRSSVKVEAE
HHHCCCCCCCCCCHH		37.8226699800
515PhosphorylationLVEGRRSSVKVEAEA
HHCCCCCCCCCCHHH		24.9327273156
517SumoylationEGRRSSVKVEAEASR
CCCCCCCCCCHHHHC		35.9821836637
517SumoylationEGRRSSVKVEAEASR
CCCCCCCCCCHHHHC		35.98-
523PhosphorylationVKVEAEASRQ-----
CCCCHHHHCC-----		23.7927486199
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
-KUbiquitinationE3 ubiquitin ligaseTOM1O60784
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAB2_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 NAB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD4_HUMANCHD4physical
16574654
CHD3_HUMANCHD3physical
16574654
TLN1_HUMANTLN1physical
22939629
PFD3_HUMANVBP1physical
22939629
NAB2_HUMANNAB2physical
25416956
CASL_HUMANNEDD9physical
25416956
PHF1_HUMANPHF1physical
25416956
PIN1_HUMANPIN1physical
25416956
RFC5_HUMANRFC5physical
25416956
JKIP2_HUMANJAKMIP2physical
25416956
MO4L1_HUMANMORF4L1physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
NDK7_HUMANNME7physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
TTC19_HUMANTTC19physical
25416956
ZBED8_HUMANZBED8physical
25416956
SCNM1_HUMANSCNM1physical
25416956
LENG1_HUMANLENG1physical
25416956
GCC1_HUMANGCC1physical
25416956
CCD33_HUMANCCDC33physical
25416956
TCHP_HUMANTCHPphysical
25416956
TF2LY_HUMANTGIF2LYphysical
25416956
ZMY19_HUMANZMYND19physical
25416956
K1C40_HUMANKRT40physical
25416956
C19L2_HUMANCWF19L2physical
25416956
TEANC_HUMANTCEANCphysical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
PHOP2_HUMANPHOSPHO2physical
25416956
CASL_HUMANNEDD9physical
21516116
NAB1_HUMANNAB1physical
28514442
NBEA_HUMANNBEAphysical
28514442
GRN_HUMANGRNphysical
28514442
TLS1_HUMANC9orf78physical
28514442
CUED2_HUMANCUEDC2physical
28514442
TNIP1_HUMANTNIP1physical
28514442
DPOD2_HUMANPOLD2physical
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 NAB2_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-6, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, 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-6; SER-162 AND SER-479,AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, 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-159 AND SER-162, ANDMASS SPECTROMETRY.

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