N42L2_HUMAN - dbPTM
N42L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID N42L2_HUMAN
UniProt AC Q92802
Protein Name NEDD4-binding protein 2-like 2
Gene Name N4BP2L2
Organism Homo sapiens (Human).
Sequence Length 583
Subcellular Localization
Protein Description
Protein Sequence MSYGEIEGKFLGPREEVTSEPRCKKLKSTTESYVFHNHSNADFHRIQEKTGNDWVPVTIIDVRGHSYLQENKIKTTDLHRPLHDEMPGNRPDVIESIDSQVLQEARPPLVSADDEIYSTSKAFIGPIYKPPEKKKRNEGRNEAHVLNGINDRGGQKEKQKFNSEKSEIDNELFQFYKEIEELEKEKDGFENSCKESEPSQEQFVPFYEGHNNGLLKPDEEKKDLSNKAMPSHCDYQQNLGNEPDKYPCNGQVIPTFCDTSFTSFRPEWQSVYPFIVPYGPPLPSLNYHLNIQRFSGPPNPPSNIFQAQDDSQIQNGYYVNNCHVNWNCMTFDQNNEYTDCSENRSSVHPSGNGCSMQDRYVSNGFCEVRERCWKDHCMDKHNGTDRFVNQQFQEEKLNKLQKLLILLRGLPGSGKTTLSRILLGQNRDGIVFSTDDYFHHQDGYRYNVNQLGDAHDWNQNRAKQAIDQGRSPVIIDNTNIQAWEMKPYVEVAIGKGYRVEFHEPETWWKFDPEELEKRNKHGVSRKKIAQMLDRYEYQMSISIVMNSVEPSHKSTQRPPPPQGRQRWGGSLGSHNRVCVTNNH
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
9SumoylationSYGEIEGKFLGPREE
CCCCCCCEECCCHHH		25.32-
9UbiquitinationSYGEIEGKFLGPREE
CCCCCCCEECCCHHH		25.32-
9SumoylationSYGEIEGKFLGPREE
CCCCCCCEECCCHHH		25.32-
18PhosphorylationLGPREEVTSEPRCKK
CCCHHHCCCCCCHHH		30.5628555341
19PhosphorylationGPREEVTSEPRCKKL
CCHHHCCCCCCHHHC		51.2621815630
20 (in isoform 3)Phosphorylation-27.6527251275
30PhosphorylationCKKLKSTTESYVFHN
HHHCCCCCCEEEEEC		29.9928555341
49UbiquitinationDFHRIQEKTGNDWVP
CCCCCHHHHCCCCEE		45.41-
72SumoylationHSYLQENKIKTTDLH
CCHHHCCCCCCCCCC		44.84-
72SumoylationHSYLQENKIKTTDLH
CCHHHCCCCCCCCCC		44.84-
106 (in isoform 3)Phosphorylation-32.39-
117PhosphorylationVSADDEIYSTSKAFI
CCCCCHHHCCCCHHH		12.12-
118PhosphorylationSADDEIYSTSKAFIG
CCCCHHHCCCCHHHC		31.69-
133AcetylationPIYKPPEKKKRNEGR
CCCCCCHHHCCCCCC		70.1725953088
163PhosphorylationKEKQKFNSEKSEIDN
HHHHCCHHCCHHHHH		49.9229083192
165SumoylationKQKFNSEKSEIDNEL
HHCCHHCCHHHHHHH		53.89-
165UbiquitinationKQKFNSEKSEIDNEL
HHCCHHCCHHHHHHH		53.89-
165SumoylationKQKFNSEKSEIDNEL
HHCCHHCCHHHHHHH		53.89-
166PhosphorylationQKFNSEKSEIDNELF
HCCHHCCHHHHHHHH		35.4129083192
174 (in isoform 3)Phosphorylation-54.0828787133
176PhosphorylationDNELFQFYKEIEELE
HHHHHHHHHHHHHHH		9.2729083192
179 (in isoform 3)Phosphorylation-4.3328787133
199PhosphorylationSCKESEPSQEQFVPF
CCCCCCCCHHHCCCC		42.1517525332
216UbiquitinationGHNNGLLKPDEEKKD
CCCCCCCCCCHHHHC		56.30-
241 (in isoform 3)Phosphorylation-61.87-
254 (in isoform 3)Phosphorylation-22.14-
345PhosphorylationTDCSENRSSVHPSGN
ECCCCCCCCCCCCCC		48.5824043423
346PhosphorylationDCSENRSSVHPSGNG
CCCCCCCCCCCCCCC		22.6224043423
350PhosphorylationNRSSVHPSGNGCSMQ
CCCCCCCCCCCCCCH		29.9724043423
355PhosphorylationHPSGNGCSMQDRYVS
CCCCCCCCCHHHHHC		22.3724043423
374UbiquitinationEVRERCWKDHCMDKH
HHHHHHHHHHHHHCC		41.02-
396 (in isoform 2)Ubiquitination-57.5221906983
396 (in isoform 1)Ubiquitination-57.5221906983
396UbiquitinationNQQFQEEKLNKLQKL
HHHHHHHHHHHHHHH		57.5221906983
399UbiquitinationFQEEKLNKLQKLLIL
HHHHHHHHHHHHHHH		63.83-
402SumoylationEKLNKLQKLLILLRG
HHHHHHHHHHHHHHC		56.55-
402UbiquitinationEKLNKLQKLLILLRG
HHHHHHHHHHHHHHC		56.55-
402SumoylationEKLNKLQKLLILLRG
HHHHHHHHHHHHHHC		56.55-
463SumoylationDWNQNRAKQAIDQGR
CCCHHHHHHHHHCCC		36.70-
463UbiquitinationDWNQNRAKQAIDQGR
CCCHHHHHHHHHCCC		36.70-
463SumoylationDWNQNRAKQAIDQGR
CCCHHHHHHHHHCCC		36.70-
467 (in isoform 3)Phosphorylation-48.1522985185
471PhosphorylationQAIDQGRSPVIIDNT
HHHHCCCCCEEECCC		30.2822210691
478PhosphorylationSPVIIDNTNIQAWEM
CCEEECCCCCCEEEE		29.9222210691
486 (in isoform 2)Ubiquitination-22.9821906983
486 (in isoform 1)Ubiquitination-22.9821906983
486UbiquitinationNIQAWEMKPYVEVAI
CCCEEEECCEEEEEE		22.9821906983
509 (in isoform 1)Ubiquitination-31.3021906983
509 (in isoform 2)Ubiquitination-31.3021906983
509UbiquitinationHEPETWWKFDPEELE
CCCCCCEECCHHHHH		31.3021906983
509MethylationHEPETWWKFDPEELE
CCCCCCEECCHHHHH		31.30-
517 (in isoform 1)Ubiquitination-74.1121906983
517 (in isoform 2)Ubiquitination-74.1121906983
517UbiquitinationFDPEELEKRNKHGVS
CCHHHHHHHHCCCCC		74.1121906983
535PhosphorylationIAQMLDRYEYQMSIS
HHHHHHHHCHHHHHE		20.75-
570PhosphorylationGRQRWGGSLGSHNRV
CCCCCCCCCCCCCCE		26.1424275569
622 (in isoform 3)Phosphorylation--
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 N42L2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of N42L2_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 N42L2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPIH_HUMANPPIHphysical
25416956
LSMD1_HUMANNAA38physical
25416956
PPIA_HUMANPPIAphysical
21516116
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of N42L2_HUMAN

loading...

Related Literatures of Post-Translational Modification
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-199, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory