BZW2_HUMAN - dbPTM
BZW2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BZW2_HUMAN
UniProt AC Q9Y6E2
Protein Name Basic leucine zipper and W2 domain-containing protein 2
Gene Name BZW2
Organism Homo sapiens (Human).
Sequence Length 419
Subcellular Localization
Protein Description May be involved in neuronal differentiation..
Protein Sequence MNKHQKPVLTGQRFKTRKRDEKEKFEPTVFRDTLVQGLNEAGDDLEAVAKFLDSTGSRLDYRRYADTLFDILVAGSMLAPGGTRIDDGDKTKMTNHCVFSANEDHETIRNYAQVFNKLIRRYKYLEKAFEDEMKKLLLFLKAFSETEQTKLAMLSGILLGNGTLPATILTSLFTDSLVKEGIAASFAVKLFKAWMAEKDANSVTSSLRKANLDKRLLELFPVNRQSVDHFAKYFTDAGLKELSDFLRVQQSLGTRKELQKELQERLSQECPIKEVVLYVKEEMKRNDLPETAVIGLLWTCIMNAVEWNKKEELVAEQALKHLKQYAPLLAVFSSQGQSELILLQKVQEYCYDNIHFMKAFQKIVVLFYKADVLSEEAILKWYKEAHVAKGKSVFLDQMKKFVEWLQNAEEESESEGEEN
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
6Ubiquitination--MNKHQKPVLTGQR
--CCCCCCCCCCCCC		36.49-
6Acetylation--MNKHQKPVLTGQR
--CCCCCCCCCCCCC		36.4926822725
10PhosphorylationKHQKPVLTGQRFKTR
CCCCCCCCCCCCCCC		31.3529496963
24UbiquitinationRKRDEKEKFEPTVFR
CCCCHHHCCCCCCHH		67.12-
24AcetylationRKRDEKEKFEPTVFR
CCCCHHHCCCCCCHH		67.1227452117
33PhosphorylationEPTVFRDTLVQGLNE
CCCCHHHHHHHHHHH		25.2721712546
55O-linked_GlycosylationVAKFLDSTGSRLDYR
HHHHHHCCCCCCCHH		38.5528510447
57PhosphorylationKFLDSTGSRLDYRRY
HHHHCCCCCCCHHHH		29.74-
57O-linked_GlycosylationKFLDSTGSRLDYRRY
HHHHCCCCCCCHHHH		29.7428510447
93SulfoxidationDDGDKTKMTNHCVFS
CCCCCCEECCCEEEE		5.7021406390
94PhosphorylationDGDKTKMTNHCVFSA
CCCCCEECCCEEEEC		24.3026126808
117UbiquitinationNYAQVFNKLIRRYKY
HHHHHHHHHHHHHHH		33.5521890473
117UbiquitinationNYAQVFNKLIRRYKY
HHHHHHHHHHHHHHH		33.5521890473
117AcetylationNYAQVFNKLIRRYKY
HHHHHHHHHHHHHHH		33.5519608861
117UbiquitinationNYAQVFNKLIRRYKY
HHHHHHHHHHHHHHH		33.5521906983
122PhosphorylationFNKLIRRYKYLEKAF
HHHHHHHHHHHHHHC		8.3026657352
123AcetylationNKLIRRYKYLEKAFE
HHHHHHHHHHHHHCH		41.3626051181
124PhosphorylationKLIRRYKYLEKAFED
HHHHHHHHHHHHCHH		15.9126657352
134AcetylationKAFEDEMKKLLLFLK
HHCHHHHHHHHHHHH		37.9227452117
135UbiquitinationAFEDEMKKLLLFLKA
HCHHHHHHHHHHHHH		42.9521890473
135UbiquitinationAFEDEMKKLLLFLKA
HCHHHHHHHHHHHHH		42.9521890473
135UbiquitinationAFEDEMKKLLLFLKA
HCHHHHHHHHHHHHH		42.9521890473
144PhosphorylationLLFLKAFSETEQTKL
HHHHHHCCCCHHHHH		48.7628102081
146PhosphorylationFLKAFSETEQTKLAM
HHHHCCCCHHHHHHH		31.9928102081
149PhosphorylationAFSETEQTKLAMLSG
HCCCCHHHHHHHHHC		23.0728102081
185PhosphorylationVKEGIAASFAVKLFK
HHHHHHHHHHHHHHH		12.5225954137
202PhosphorylationMAEKDANSVTSSLRK
HHHCCHHHHHHHHHH		28.6125159151
204PhosphorylationEKDANSVTSSLRKAN
HCCHHHHHHHHHHCC		16.6621712546
205PhosphorylationKDANSVTSSLRKANL
CCHHHHHHHHHHCCC		25.8125627689
206PhosphorylationDANSVTSSLRKANLD
CHHHHHHHHHHCCCC		23.8725627689
226PhosphorylationLFPVNRQSVDHFAKY
HCCCCHHHHHHHHHH		26.6927251275
232UbiquitinationQSVDHFAKYFTDAGL
HHHHHHHHHHHHHCH		39.7021890473
232UbiquitinationQSVDHFAKYFTDAGL
HHHHHHHHHHHHHCH		39.7021890473
240UbiquitinationYFTDAGLKELSDFLR
HHHHHCHHHHHHHHH		56.5421890473
243PhosphorylationDAGLKELSDFLRVQQ
HHCHHHHHHHHHHHH		27.66-
260AcetylationGTRKELQKELQERLS
CCHHHHHHHHHHHHH		73.3727452117
260UbiquitinationGTRKELQKELQERLS
CCHHHHHHHHHHHHH		73.37-
267PhosphorylationKELQERLSQECPIKE
HHHHHHHHCCCCHHH		30.10-
310UbiquitinationNAVEWNKKEELVAEQ
HHHHCCHHHHHHHHH		53.89-
320UbiquitinationLVAEQALKHLKQYAP
HHHHHHHHHHHHHHH		50.3221890473
320UbiquitinationLVAEQALKHLKQYAP
HHHHHHHHHHHHHHH		50.3221890473
358UbiquitinationYDNIHFMKAFQKIVV
HHCHHHHHHHHHHHH		45.1421890473
358UbiquitinationYDNIHFMKAFQKIVV
HHCHHHHHHHHHHHH		45.1421890473
383UbiquitinationEAILKWYKEAHVAKG
HHHHHHHHHHHHHCC		47.51-
391AcetylationEAHVAKGKSVFLDQM
HHHHHCCCCHHHHHH		42.6227452117
391MalonylationEAHVAKGKSVFLDQM
HHHHHCCCCHHHHHH		42.6226320211
392PhosphorylationAHVAKGKSVFLDQMK
HHHHCCCCHHHHHHH		27.1128348404
412PhosphorylationLQNAEEESESEGEEN
HHHHHHHHHHCCCCC		50.1020201521
414PhosphorylationNAEEESESEGEEN--
HHHHHHHHCCCCC--		61.2520201521
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 BZW2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BZW2_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 BZW2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABHEA_HUMANABHD14Aphysical
22863883
PSF3_HUMANGINS3physical
22863883
PA1B2_HUMANPAFAH1B2physical
22863883
EIF2A_HUMANEIF2Aphysical
21745818
EI2BA_HUMANEIF2B1physical
21745818
EIF3A_HUMANEIF3Aphysical
21745818
IF2G_YEASTGCD11physical
21745818
IF2A_YEASTSUI2physical
21745818
EIF3B_YEASTPRT1physical
21745818
EI2BE_YEASTGCD6genetic
21745818
MUL1_HUMANMUL1physical
28514442
EXOG_HUMANEXOGphysical
28514442
5NT3A_HUMANNT5C3Aphysical
28514442
CANT1_HUMANCANT1physical
28514442
ENDD1_HUMANENDOD1physical
28514442
TMM43_HUMANTMEM43physical
28514442
ZFPL1_HUMANZFPL1physical
28514442
SCPDL_HUMANSCCPDHphysical
28514442
MRS2_HUMANMRS2physical
28514442
MAVS_HUMANMAVSphysical
28514442
OMA1_HUMANOMA1physical
28514442
TV23C_HUMANTVP23Cphysical
28514442
NXT1_HUMANNXT1physical
28514442
RRAS_HUMANRRASphysical
28514442
RASN_HUMANNRASphysical
28514442
S27A2_HUMANSLC27A2physical
28514442
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 BZW2_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-117, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-414, ANDMASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-414, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-414, ANDMASS SPECTROMETRY.
"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-412 AND SER-414, ANDMASS SPECTROMETRY.

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