NAB1_HUMAN - dbPTM
NAB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAB1_HUMAN
UniProt AC Q13506
Protein Name NGFI-A-binding protein 1
Gene Name NAB1
Organism Homo sapiens (Human).
Sequence Length 487
Subcellular Localization Nucleus.
Protein Description Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2..
Protein Sequence MAAALPRTLGELQLYRILQKANLLSYFDAFIQQGGDDVQQLCEAGEEEFLEIMALVGMASKPLHVRRLQKALRDWVTNPGLFNQPLTSLPVSSIPIYKLPEGSPTWLGISCSSYERSSNAREPHLKIPKCAATTCVQSLGQGKSDVVGSLALQSVGESRLWQGHHATESEHSLSPADLGSPASPKESSEALDAAAALSVAECVERMAPTLPKSDLNEVKELLKTNKKLAKMIGHIFEMNDDDPHKEEEIRKYSAIYGRFDSKRKDGKHLTLHELTVNEAAAQLCVKDNALLTRRDELFALARQISREVTYKYTYRTTKSKCGERDELSPKRIKVEDGFPDFQDSVQTLFQQARAKSEELAALSSQQPEKVMAKQMEFLCNQAGYERLQHAERRLSAGLYRQSSEEHSPNGLTSDNSDGQGERPLNLRMPNLQNRQPHHFVVDGELSRLYPSEAKSHSSESLGILKDYPHSAFTLEKKVIKTEPEDSR
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
60PhosphorylationMALVGMASKPLHVRR
HHHHHHCCCHHHHHH		26.3924719451
103PhosphorylationIYKLPEGSPTWLGIS
CEECCCCCCCEEEEE		19.9321815630
105PhosphorylationKLPEGSPTWLGISCS
ECCCCCCCEEEEECC		34.7121815630
126SumoylationNAREPHLKIPKCAAT
CCCCCCCCCCHHHHH		54.6628112733
129SumoylationEPHLKIPKCAATTCV
CCCCCCCHHHHHHHH		39.7228112733
129SumoylationEPHLKIPKCAATTCV
CCCCCCCHHHHHHHH		39.72-
129UbiquitinationEPHLKIPKCAATTCV
CCCCCCCHHHHHHHH		39.72-
143SumoylationVQSLGQGKSDVVGSL
HHHHCCCCCCHHHEE		35.2828112733
167PhosphorylationLWQGHHATESEHSLS
CCCCCCCCCCCCCCC		35.3720068231
169PhosphorylationQGHHATESEHSLSPA
CCCCCCCCCCCCCHH		35.9320068231
172PhosphorylationHATESEHSLSPADLG
CCCCCCCCCCHHHCC		26.8723927012
174PhosphorylationTESEHSLSPADLGSP
CCCCCCCCHHHCCCC		22.5123927012
180PhosphorylationLSPADLGSPASPKES
CCHHHCCCCCCHHHH		25.2923927012
183PhosphorylationADLGSPASPKESSEA
HHCCCCCCHHHHHHH		39.6328731282
187PhosphorylationSPASPKESSEALDAA
CCCCHHHHHHHHHHH		39.3426074081
188PhosphorylationPASPKESSEALDAAA
CCCHHHHHHHHHHHH		28.1626074081
212SumoylationRMAPTLPKSDLNEVK
HHCCCCCHHHHHHHH		60.7728112733
212SumoylationRMAPTLPKSDLNEVK
HHCCCCCHHHHHHHH		60.77-
219UbiquitinationKSDLNEVKELLKTNK
HHHHHHHHHHHHHHH		36.14-
312PhosphorylationSREVTYKYTYRTTKS
CHHHCHHEEEECCCC		9.8929083192
313PhosphorylationREVTYKYTYRTTKSK
HHHCHHEEEECCCCC		11.4529083192
314PhosphorylationEVTYKYTYRTTKSKC
HHCHHEEEECCCCCC		11.6729083192
316PhosphorylationTYKYTYRTTKSKCGE
CHHEEEECCCCCCCC		28.3229083192
317PhosphorylationYKYTYRTTKSKCGER
HHEEEECCCCCCCCC		25.0729083192
319PhosphorylationYTYRTTKSKCGERDE
EEEECCCCCCCCCCC		30.9629083192
328PhosphorylationCGERDELSPKRIKVE
CCCCCCCCCCCEEEC		26.7425159151
333SumoylationELSPKRIKVEDGFPD
CCCCCCEEECCCCCC		43.5421836637
333SumoylationELSPKRIKVEDGFPD
CCCCCCEEECCCCCC		43.54-
355SumoylationLFQQARAKSEELAAL
HHHHHHHHHHHHHHH		53.5028112733
355SumoylationLFQQARAKSEELAAL
HHHHHHHHHHHHHHH		53.50-
355UbiquitinationLFQQARAKSEELAAL
HHHHHHHHHHHHHHH		53.50-
356PhosphorylationFQQARAKSEELAALS
HHHHHHHHHHHHHHH		35.0125850435
369SumoylationLSSQQPEKVMAKQME
HHCCCHHHHHHHHHH		43.9528112733
369SumoylationLSSQQPEKVMAKQME
HHCCCHHHHHHHHHH		43.95-
373SumoylationQPEKVMAKQMEFLCN
CHHHHHHHHHHHHHH		31.89-
373SumoylationQPEKVMAKQMEFLCN
CHHHHHHHHHHHHHH		31.8928112733
395PhosphorylationQHAERRLSAGLYRQS
HHHHHHHHHCCCCCC		20.6223927012
399PhosphorylationRRLSAGLYRQSSEEH
HHHHHCCCCCCCCCC		12.9923186163
402PhosphorylationSAGLYRQSSEEHSPN
HHCCCCCCCCCCCCC		30.6230266825
403PhosphorylationAGLYRQSSEEHSPNG
HCCCCCCCCCCCCCC		38.3730266825
407PhosphorylationRQSSEEHSPNGLTSD
CCCCCCCCCCCCCCC		24.2830266825
412PhosphorylationEHSPNGLTSDNSDGQ
CCCCCCCCCCCCCCC		35.1223663014
413PhosphorylationHSPNGLTSDNSDGQG
CCCCCCCCCCCCCCC		39.5817081983
416PhosphorylationNGLTSDNSDGQGERP
CCCCCCCCCCCCCCC		48.3725850435
454SumoylationRLYPSEAKSHSSESL
HHCCHHHHCCCCCCC		44.65-
454SumoylationRLYPSEAKSHSSESL
HHCCHHHHCCCCCCC		44.6528112733
455PhosphorylationLYPSEAKSHSSESLG
HCCHHHHCCCCCCCC		35.3328348404
457PhosphorylationPSEAKSHSSESLGIL
CHHHHCCCCCCCCCC		42.7825159151
458PhosphorylationSEAKSHSSESLGILK
HHHHCCCCCCCCCCC		26.2728348404
460PhosphorylationAKSHSSESLGILKDY
HHCCCCCCCCCCCCC		33.5728348404
465SumoylationSESLGILKDYPHSAF
CCCCCCCCCCCCCCE		53.9828112733
465SumoylationSESLGILKDYPHSAF
CCCCCCCCCCCCCCE		53.98-
465UbiquitinationSESLGILKDYPHSAF
CCCCCCCCCCCCCCE		53.98-
470PhosphorylationILKDYPHSAFTLEKK
CCCCCCCCCEEEEEE		22.1528555341
473PhosphorylationDYPHSAFTLEKKVIK
CCCCCCEEEEEEEEC		33.4528555341
476UbiquitinationHSAFTLEKKVIKTEP
CCCEEEEEEEECCCC		56.29-
477SumoylationSAFTLEKKVIKTEPE
CCEEEEEEEECCCCC		39.5628112733
477SumoylationSAFTLEKKVIKTEPE
CCEEEEEEEECCCCC		39.56-
480SumoylationTLEKKVIKTEPEDSR
EEEEEEECCCCCCCC		50.2321836637
480SumoylationTLEKKVIKTEPEDSR
EEEEEEECCCCCCCC		50.23-
486PhosphorylationIKTEPEDSR------
ECCCCCCCC------		37.9224719451
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 NAB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAB1_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 NAB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EGR1_HUMANEGR1physical
7624335
OBF1_HUMANPOU2AF1physical
20211142
CHD4_HUMANCHD4physical
16574654
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 NAB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-328, AND MASSSPECTROMETRY.

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