NIF3L_HUMAN - dbPTM
NIF3L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NIF3L_HUMAN
UniProt AC Q9GZT8
Protein Name NIF3-like protein 1 {ECO:0000305|PubMed:11124544}
Gene Name NIF3L1 {ECO:0000312|HGNC:HGNC:13390}
Organism Homo sapiens (Human).
Sequence Length 377
Subcellular Localization Cytoplasm . Nucleus . Interaction with COPS2 may regulate localization to the nucleus.
Protein Description May function as a transcriptional corepressor through its interaction with COPS2, negatively regulating the expression of genes involved in neuronal differentiation..
Protein Sequence MLSSCVRPVPTTVRFVDSLICNSSRSFMDLKALLSSLNDFASLSFAESWDNVGLLVEPSPPHTVNTLFLTNDLTEEVMEEVLQKKADLILSYHPPIFRPMKRITWNTWKERLVIRALENRVGIYSPHTAYDAAPQGVNNWLAKGLGACTSRPIHPSKAPNYPTEGNHRVEFNVNYTQDLDKVMSAVKGIDGVSVTSFSARTGNEEQTRINLNCTQKALMQVVDFLSRNKQLYQKTEILSLEKPLLLHTGMGRLCTLDESVSLATMIDRIKRHLKLSHIRLALGVGRTLESQVKVVALCAGSGSSVLQGVEADLYLTGEMSHHDTLDAASQGINVILCEHSNTERGFLSDLRDMLDSHLENKINIILSETDRDPLQVV
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
82 (in isoform 2)Ubiquitination-7.5521890473
101AcetylationPPIFRPMKRITWNTW
CCCCCCCCCCCCCCH		43.2425953088
104PhosphorylationFRPMKRITWNTWKER
CCCCCCCCCCCHHHH		19.3924719451
109AcetylationRITWNTWKERLVIRA
CCCCCCHHHHHHHHH		30.8019608861
109UbiquitinationRITWNTWKERLVIRA
CCCCCCHHHHHHHHH		30.8021890473
109 (in isoform 1)Ubiquitination-30.8021890473
109UbiquitinationRITWNTWKERLVIRA
CCCCCCHHHHHHHHH		30.8021890473
124PhosphorylationLENRVGIYSPHTAYD
HHHCCCCCCCCCHHH		15.38-
125PhosphorylationENRVGIYSPHTAYDA
HHCCCCCCCCCHHHC		14.32-
130PhosphorylationIYSPHTAYDAAPQGV
CCCCCCHHHCCCCCH		13.7925839225
143UbiquitinationGVNNWLAKGLGACTS
CHHHHHHHCCCCCCC		53.12-
157UbiquitinationSRPIHPSKAPNYPTE
CCCCCCCCCCCCCCC		72.77-
161PhosphorylationHPSKAPNYPTEGNHR
CCCCCCCCCCCCCCC		15.5226437602
181UbiquitinationNYTQDLDKVMSAVKG
ECCCCHHHHHHHHCC		47.32-
181AcetylationNYTQDLDKVMSAVKG
ECCCCHHHHHHHHCC		47.3225038526
187UbiquitinationDKVMSAVKGIDGVSV
HHHHHHHCCCCCEEE		50.28-
207 (in isoform 2)Ubiquitination-36.4721890473
215 (in isoform 2)Ubiquitination-31.0921890473
216UbiquitinationINLNCTQKALMQVVD
EECCCHHHHHHHHHH		25.90-
219SulfoxidationNCTQKALMQVVDFLS
CCHHHHHHHHHHHHH		3.2130846556
226PhosphorylationMQVVDFLSRNKQLYQ
HHHHHHHHHCHHHHH		33.5321712546
229UbiquitinationVDFLSRNKQLYQKTE
HHHHHHCHHHHHHHC		40.34-
234 (in isoform 1)Ubiquitination-34.2721890473
234UbiquitinationRNKQLYQKTEILSLE
HCHHHHHHHCEECCC		34.2721890473
234UbiquitinationRNKQLYQKTEILSLE
HCHHHHHHHCEECCC		34.2721890473
242UbiquitinationTEILSLEKPLLLHTG
HCEECCCCCEEHHCC		46.3821890473
242 (in isoform 1)Ubiquitination-46.3821890473
242AcetylationTEILSLEKPLLLHTG
HCEECCCCCEEHHCC		46.3825038526
2422-HydroxyisobutyrylationTEILSLEKPLLLHTG
HCEECCCCCEEHHCC		46.38-
255PhosphorylationTGMGRLCTLDESVSL
CCCCCCCCCCHHHHH		41.6623403867
259PhosphorylationRLCTLDESVSLATMI
CCCCCCHHHHHHHHH		19.37-
261PhosphorylationCTLDESVSLATMIDR
CCCCHHHHHHHHHHH		22.9019664994
264PhosphorylationDESVSLATMIDRIKR
CHHHHHHHHHHHHHH		21.6923403867
276PhosphorylationIKRHLKLSHIRLALG
HHHHHCHHHHHHHHH		18.4520068231
348PhosphorylationNTERGFLSDLRDMLD
CCCCCHHHHHHHHHH		32.1324719451
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 NIF3L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NIF3L_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 NIF3L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THOC7_HUMANTHOC7physical
12951069
BEND7_HUMANBEND7physical
16189514
NIF3L_HUMANNIF3L1physical
16189514
TIFA_HUMANTIFAphysical
16189514
KCD17_HUMANKCTD17physical
16189514
DMRTB_HUMANDMRTB1physical
16189514
KXDL1_HUMANKXD1physical
16189514
DCTP1_HUMANDCTPP1physical
16189514
T22D4_HUMANTSC22D4physical
16189514
1433T_HUMANYWHAQphysical
15163635
NIF3L_HUMANNIF3L1physical
12951069
TACC1_HUMANTACC1physical
22939629
PALM2_HUMANPALM2physical
22939629
PPAL_HUMANACP2physical
22939629
PLXB2_HUMANPLXNB2physical
22939629
NT5D1_HUMANNT5DC1physical
22939629
BEND7_HUMANBEND7physical
19060904
PRAF1_HUMANRABAC1physical
19060904
DMRTB_HUMANDMRTB1physical
19060904
PCH2_HUMANTRIP13physical
19060904
DHYS_HUMANDHPSphysical
19060904
MTNB_HUMANAPIPphysical
19060904
FSBP_HUMANRAD54Bphysical
19060904
RA54B_HUMANRAD54Bphysical
19060904
NDKA_HUMANNME1physical
19060904
PUR6_HUMANPAICSphysical
19060904
SAT1_HUMANSAT1physical
19060904
STAT3_HUMANSTAT3physical
21988832
AGFG1_HUMANAGFG1physical
22863883
ARPC2_HUMANARPC2physical
22863883
FUBP1_HUMANFUBP1physical
22863883
GRPE1_HUMANGRPEL1physical
22863883
AMPL_HUMANLAP3physical
22863883
PP2AA_HUMANPPP2CAphysical
22863883
RAGP1_HUMANRANGAP1physical
22863883
SH3G1_HUMANSH3GL1physical
22863883
SHLB1_HUMANSH3GLB1physical
22863883
TPD54_HUMANTPD52L2physical
22863883
NIF3L_HUMANNIF3L1physical
25416956
C102B_HUMANCCDC102Bphysical
25416956
AP5B1_HUMANAP5B1physical
25416956
NUD14_HUMANNUDT14physical
25416956
NATD1_HUMANNATD1physical
25416956
ARPIN_HUMANARPINphysical
25416956
PEPL1_HUMANNPEPL1physical
26344197
PNMA1_HUMANPNMA1physical
21516116
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 NIF3L_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109, AND MASS SPECTROMETRY.

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