KANL2_HUMAN - dbPTM
KANL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KANL2_HUMAN
UniProt AC Q9H9L4
Protein Name KAT8 regulatory NSL complex subunit 2
Gene Name KANSL2
Organism Homo sapiens (Human).
Sequence Length 492
Subcellular Localization Nucleus .
Protein Description As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription..
Protein Sequence MNRIRIHVLPTNRGRITPVPRSQEPLSCAFTHRPCSHPRLEGQEFCIKHILEDKNAPFKQCSYISTKNGKRCPNAAPKPEKKDGVSFCAEHVRRNALALHAQMKKTNPGPVGETLLCQLSSYAKTELGSQTPESSRSEASRILDEDSWSDGEQEPITVDQTWRGDPDSEADSIDSDQEDPLKHAGVYTAEEVALIMREKLIRLQSLYIDQFKRLQHLLKEKKRRYLHNRKVEHEALGSSLLTGPEGLLAKERENLKRLKCLRRYRQRYGVEALLHRQLKERRMLATDGAAQQAHTTRSSQRCLAFVDDVRCSNQSLPMTRHCLTHICQDTNQVLFKCCQGSEEVPCNKPVPVSLSEDPCCPLHFQLPPQMYKPEQVLSVPDDLEAGPMDLYLSAAELQPTESLPLEFSDDLDVVGDGMQCPPSPLLFDPSLTLEDHLVKEIAEDPVDILGQMQMAGDGCRSQGSRNSEKASAPLSQSGLATANGKPEPTSIS
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
17PhosphorylationPTNRGRITPVPRSQE
CCCCCCCCCCCCCCC		19.5130266825
22PhosphorylationRITPVPRSQEPLSCA
CCCCCCCCCCCCEEE		32.5920068231
27PhosphorylationPRSQEPLSCAFTHRP
CCCCCCCEEEECCCC		17.7020068231
31PhosphorylationEPLSCAFTHRPCSHP
CCCEEEECCCCCCCC		9.8420068231
36PhosphorylationAFTHRPCSHPRLEGQ
EECCCCCCCCCCCCH		38.9330631047
54SumoylationIKHILEDKNAPFKQC
HHHHHCCCCCCHHHC		45.71-
54SumoylationIKHILEDKNAPFKQC
HHHHHCCCCCCHHHC		45.71-
54UbiquitinationIKHILEDKNAPFKQC
HHHHHCCCCCCHHHC		45.7129967540
78SumoylationRCPNAAPKPEKKDGV
CCCCCCCCCCCCCCC		62.17-
78SumoylationRCPNAAPKPEKKDGV
CCCCCCCCCCCCCCC		62.1728112733
106PhosphorylationLHAQMKKTNPGPVGE
HHHHHHHCCCCCCCH		40.9221712546
114PhosphorylationNPGPVGETLLCQLSS
CCCCCCHHHHHHHHH		21.07-
120PhosphorylationETLLCQLSSYAKTEL
HHHHHHHHHHHCCCC		8.74-
125PhosphorylationQLSSYAKTELGSQTP
HHHHHHCCCCCCCCC		28.4223312004
129PhosphorylationYAKTELGSQTPESSR
HHCCCCCCCCCCCCH		43.4325262027
131PhosphorylationKTELGSQTPESSRSE
CCCCCCCCCCCCHHH		30.6229255136
134PhosphorylationLGSQTPESSRSEASR
CCCCCCCCCHHHHHH		32.0529255136
135PhosphorylationGSQTPESSRSEASRI
CCCCCCCCHHHHHHH		37.8629255136
137PhosphorylationQTPESSRSEASRILD
CCCCCCHHHHHHHCC		39.1923312004
140PhosphorylationESSRSEASRILDEDS
CCCHHHHHHHCCCCC		18.7923312004
147PhosphorylationSRILDEDSWSDGEQE
HHHCCCCCCCCCCCC		26.8225159151
149PhosphorylationILDEDSWSDGEQEPI
HCCCCCCCCCCCCCE		39.4225159151
157PhosphorylationDGEQEPITVDQTWRG
CCCCCCEECCCCCCC		28.8430108239
161PhosphorylationEPITVDQTWRGDPDS
CCEECCCCCCCCCCC		16.8023927012
168PhosphorylationTWRGDPDSEADSIDS
CCCCCCCCCCCCCCC		39.8225159151
172PhosphorylationDPDSEADSIDSDQED
CCCCCCCCCCCCCCC		35.0325159151
175PhosphorylationSEADSIDSDQEDPLK
CCCCCCCCCCCCHHH		39.2525159151
238PhosphorylationVEHEALGSSLLTGPE
CCHHHHCCHHHHCHH		20.7521712546
239PhosphorylationEHEALGSSLLTGPEG
CHHHHCCHHHHCHHH		26.1221712546
242PhosphorylationALGSSLLTGPEGLLA
HHCCHHHHCHHHHHH		56.8628555341
250UbiquitinationGPEGLLAKERENLKR
CHHHHHHHHHHHHHH		58.2229967540
286PhosphorylationKERRMLATDGAAQQA
HHHHHHHCCHHHHHH		30.88-
315PhosphorylationDVRCSNQSLPMTRHC
EECCCCCCCCCHHHH		38.4026434552
319PhosphorylationSNQSLPMTRHCLTHI
CCCCCCCHHHHHHHH		18.4726434552
330PhosphorylationLTHICQDTNQVLFKC
HHHHHCCCCCHHHHH		11.1526434552
423PhosphorylationDGMQCPPSPLLFDPS
CCCCCCCCCCCCCCC		17.2126074081
461PhosphorylationMAGDGCRSQGSRNSE
CCCCCCCCCCCCCCC		42.8623312004
464PhosphorylationDGCRSQGSRNSEKAS
CCCCCCCCCCCCCCC		22.2023312004
467PhosphorylationRSQGSRNSEKASAPL
CCCCCCCCCCCCCCH		39.0923312004
471PhosphorylationSRNSEKASAPLSQSG
CCCCCCCCCCHHHHC		41.3023312004
475PhosphorylationEKASAPLSQSGLATA
CCCCCCHHHHCCCCC		22.6523312004
477PhosphorylationASAPLSQSGLATANG
CCCCHHHHCCCCCCC		32.1923312004
481PhosphorylationLSQSGLATANGKPEP
HHHHCCCCCCCCCCC		26.2123312004
485AcetylationGLATANGKPEPTSIS
CCCCCCCCCCCCCCC		46.1226051181
489PhosphorylationANGKPEPTSIS----
CCCCCCCCCCC----		36.7123312004
490PhosphorylationNGKPEPTSIS-----
CCCCCCCCCC-----		31.3923312004
492PhosphorylationKPEPTSIS-------
CCCCCCCC-------		33.6623312004
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 KANL2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KANL2_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 KANL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
NEMO_HUMANIKBKGphysical
21988832
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 KANL2_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-168; SER-172 ANDSER-175, AND MASS SPECTROMETRY.

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