NLE1_HUMAN - dbPTM
NLE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NLE1_HUMAN
UniProt AC Q9NVX2
Protein Name Notchless protein homolog 1
Gene Name NLE1
Organism Homo sapiens (Human).
Sequence Length 485
Subcellular Localization Nucleus, nucleolus .
Protein Description Plays a role in regulating Notch activity. Plays a role in regulating the expression of CDKN1A and several members of the Wnt pathway, probably via its effects on Notch activity. Required during embryogenesis for inner mass cell survival (By similarity)..
Protein Sequence MAAAVPDEAVARDVQRLLVQFQDEGGQLLGSPFDVPVDITPDRLQLVCNALLAQEDPLPLAFFVHDAEIVSSLGKTLESQAVETEKVLDIIYQPQAIFRVRAVTRCTSSLEGHSEAVISVAFSPTGKYLASGSGDTTVRFWDLSTETPHFTCKGHRHWVLSISWSPDGRKLASGCKNGQILLWDPSTGKQVGRTLAGHSKWITGLSWEPLHANPECRYVASSSKDGSVRIWDTTAGRCERILTGHTQSVTCLRWGGDGLLYSASQDRTIKVWRAHDGVLCRTLQGHGHWVNTMALSTDYALRTGAFEPAEASVNPQDLQGSLQELKERALSRYNLVRGQGPERLVSGSDDFTLFLWSPAEDKKPLTRMTGHQALINQVLFSPDSRIVASASFDKSIKLWDGRTGKYLASLRGHVAAVYQIAWSADSRLLVSGSSDSTLKVWDVKAQKLAMDLPGHADEVYAVDWSPDGQRVASGGKDKCLRIWRR
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------MAAAVPDEA
------CCCCCCHHH		12.2522223895
31PhosphorylationEGGQLLGSPFDVPVD
CCCCCCCCCCCCCCC		23.5128348404
34 (in isoform 2)Ubiquitination-47.39-
34UbiquitinationQLLGSPFDVPVDITP
CCCCCCCCCCCCCCH		47.3921963094
40PhosphorylationFDVPVDITPDRLQLV
CCCCCCCCHHHHHHH		18.0520068231
79PhosphorylationSLGKTLESQAVETEK
HHCCHHHHHCCCCHH		26.9317525332
92PhosphorylationEKVLDIIYQPQAIFR
HHHHHHHHCCCEEEE		17.9327642862
128PhosphorylationAFSPTGKYLASGSGD
EECCCCCCCCCCCCC		14.6228152594
131PhosphorylationPTGKYLASGSGDTTV
CCCCCCCCCCCCCEE		30.7820068231
133PhosphorylationGKYLASGSGDTTVRF
CCCCCCCCCCCEEEE		30.8820068231
136PhosphorylationLASGSGDTTVRFWDL
CCCCCCCCEEEEEEC		30.6220068231
137PhosphorylationASGSGDTTVRFWDLS
CCCCCCCEEEEEECC		17.9020068231
152UbiquitinationTETPHFTCKGHRHWV
CCCCCEEECCCCEEE		4.9329967540
155UbiquitinationPHFTCKGHRHWVLSI
CCEEECCCCEEEEEE		12.1529967540
161PhosphorylationGHRHWVLSISWSPDG
CCCEEEEEEEECCCC		12.6420068231
176UbiquitinationRKLASGCKNGQILLW
CCCCCCCCCCEEEEE		68.58-
184UbiquitinationNGQILLWDPSTGKQV
CCEEEEECCCCCCCC		27.5224816145
189UbiquitinationLWDPSTGKQVGRTLA
EECCCCCCCCCCCCC		41.7329967540
224UbiquitinationRYVASSSKDGSVRIW
EEEEECCCCCCEEEE		68.9721906983
243PhosphorylationGRCERILTGHTQSVT
CCEEEEEECCCCEEE		25.2520068231
246PhosphorylationERILTGHTQSVTCLR
EEEEECCCCEEEEEE		24.7220068231
248PhosphorylationILTGHTQSVTCLRWG
EEECCCCEEEEEEEC		22.1320068231
250PhosphorylationTGHTQSVTCLRWGGD
ECCCCEEEEEEECCC		15.8620068231
326UbiquitinationQGSLQELKERALSRY
HHHHHHHHHHHHHHH		44.3921906983
369PhosphorylationKKPLTRMTGHQALIN
CCCCCHHCCHHHHHH		28.3720068231
381PhosphorylationLINQVLFSPDSRIVA
HHHHHHCCCCCCEEE		24.5220068231
384PhosphorylationQVLFSPDSRIVASAS
HHHCCCCCCEEEECC		27.5620068231
394AcetylationVASASFDKSIKLWDG
EEECCCCCCEEEECC		52.6626051181
397AcetylationASFDKSIKLWDGRTG
CCCCCCEEEECCCCH		51.0925953088
405AcetylationLWDGRTGKYLASLRG
EECCCCHHHHHHHHH		36.1625953088
409PhosphorylationRTGKYLASLRGHVAA
CCHHHHHHHHHHHEE		18.9224719451
439UbiquitinationGSSDSTLKVWDVKAQ
CCCCCCEEEEECCHH		41.17-
444UbiquitinationTLKVWDVKAQKLAMD
CEEEEECCHHEEECC		42.5029967540
447UbiquitinationVWDVKAQKLAMDLPG
EEECCHHEEECCCCC		42.9729967540
476UbiquitinationQRVASGGKDKCLRIW
CCCCCCCCCCEEEEC		58.5024816145
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 NLE1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NLE1_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 NLE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR5_HUMANWDR5physical
17041588
GLGB_HUMANGBE1physical
26344197
HNRH3_HUMANHNRNPH3physical
26344197
C1TC_HUMANMTHFD1physical
26344197
SPAG7_HUMANSPAG7physical
26344197
NLE1_HUMANNLE1physical
26472760
TCPB_HUMANCCT2physical
26472760
TCPD_HUMANCCT4physical
26472760
TCPZ_HUMANCCT6Aphysical
26472760
TCPE_HUMANCCT5physical
26472760
TCPH_HUMANCCT7physical
26472760
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 NLE1_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, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASSSPECTROMETRY.

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