BZW1_HUMAN - dbPTM
BZW1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BZW1_HUMAN
UniProt AC Q7L1Q6
Protein Name Basic leucine zipper and W2 domain-containing protein 1
Gene Name BZW1
Organism Homo sapiens (Human).
Sequence Length 419
Subcellular Localization
Protein Description Enhances histone H4 gene transcription but does not seem to bind DNA directly..
Protein Sequence MNNQKQQKPTLSGQRFKTRKRDEKERFDPTQFQDCIIQGLTETGTDLEAVAKFLDASGAKLDYRRYAETLFDILVAGGMLAPGGTLADDMMRTDVCVFAAQEDLETMQAFAQVFNKLIRRYKYLEKGFEDEVKKLLLFLKGFSESERNKLAMLTGVLLANGTLNASILNSLYNENLVKEGVSAAFAVKLFKSWINEKDINAVAASLRKVSMDNRLMELFPANKQSVEHFTKYFTEAGLKELSEYVRNQQTIGARKELQKELQEQMSRGDPFKDIILYVKEEMKKNNIPEPVVIGIVWSSVMSTVEWNKKEELVAEQAIKHLKQYSPLLAAFTTQGQSELTLLLKIQEYCYDNIHFMKAFQKIVVLFYKAEVLSEEPILKWYKDAHVAKGKSVFLEQMKKFVEWLKNAEEESESEAEEGD
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
1Acetylation-------MNNQKQQK
-------CCCCCCCC		10.8322814378
5Ubiquitination---MNNQKQQKPTLS
---CCCCCCCCCCCC		57.74-
8UbiquitinationMNNQKQQKPTLSGQR
CCCCCCCCCCCCCHH		37.16-
10PhosphorylationNQKQQKPTLSGQRFK
CCCCCCCCCCCHHHC		40.3620068231
12PhosphorylationKQQKPTLSGQRFKTR
CCCCCCCCCHHHCCC		35.0425159151
24UbiquitinationKTRKRDEKERFDPTQ
CCCCCCHHHCCCHHH		59.48-
37 (in isoform 3)Ubiquitination-3.14-
40 (in isoform 3)Ubiquitination-1.93-
44 (in isoform 3)Phosphorylation-15.8224719451
52UbiquitinationTDLEAVAKFLDASGA
CCHHHHHHHHCCCCC		39.60-
60AcetylationFLDASGAKLDYRRYA
HHCCCCCCCCHHHHH		45.4726051181
60MalonylationFLDASGAKLDYRRYA
HHCCCCCCCCHHHHH		45.4726320211
60UbiquitinationFLDASGAKLDYRRYA
HHCCCCCCCCHHHHH		45.47-
60 (in isoform 1)Ubiquitination-45.4721890473
60 (in isoform 2)Ubiquitination-45.4721890473
64UbiquitinationSGAKLDYRRYAETLF
CCCCCCHHHHHHHHH		25.4621890473
92UbiquitinationTLADDMMRTDVCVFA
CCHHHHHHCCHHHEE		22.5721890473
92 (in isoform 3)Malonylation-22.5726320211
92 (in isoform 3)Ubiquitination-22.57-
126AcetylationRRYKYLEKGFEDEVK
HHHHHHHCCCHHHHH		67.3227452117
126UbiquitinationRRYKYLEKGFEDEVK
HHHHHHHCCCHHHHH		67.32-
133AcetylationKGFEDEVKKLLLFLK
CCCHHHHHHHHHHHH		35.3427452117
134UbiquitinationGFEDEVKKLLLFLKG
CCHHHHHHHHHHHHC		49.93-
140UbiquitinationKKLLLFLKGFSESER
HHHHHHHHCCCHHHH		51.0421890473
140 (in isoform 1)Ubiquitination-51.0421890473
140 (in isoform 2)Ubiquitination-51.0421890473
144UbiquitinationLFLKGFSESERNKLA
HHHHCCCHHHHHHHH		55.1221890473
152SulfoxidationSERNKLAMLTGVLLA
HHHHHHHHHHHHHHH		5.0828183972
172UbiquitinationASILNSLYNENLVKE
HHHHHHHHCCCCHHH		21.9121890473
182PhosphorylationNLVKEGVSAAFAVKL
CCHHHCHHHHHHHHH		25.4120068231
188UbiquitinationVSAAFAVKLFKSWIN
HHHHHHHHHHHHHCC		44.79-
191UbiquitinationAFAVKLFKSWINEKD
HHHHHHHHHHCCHHH		56.1521890473
191 (in isoform 1)Ubiquitination-56.1521890473
191 (in isoform 2)Ubiquitination-56.1521890473
192PhosphorylationFAVKLFKSWINEKDI
HHHHHHHHHCCHHHH		26.3422210691
195UbiquitinationKLFKSWINEKDINAV
HHHHHHCCHHHHHHH		43.9621890473
197UbiquitinationFKSWINEKDINAVAA
HHHHCCHHHHHHHHH		60.4621890473
197 (in isoform 1)Ubiquitination-60.4621890473
197 (in isoform 2)Ubiquitination-60.4621890473
201UbiquitinationINEKDINAVAASLRK
CCHHHHHHHHHHHHH		7.8321890473
205PhosphorylationDINAVAASLRKVSMD
HHHHHHHHHHHHCCC		20.9721712546
208UbiquitinationAVAASLRKVSMDNRL
HHHHHHHHHCCCCHH		43.91-
210PhosphorylationAASLRKVSMDNRLME
HHHHHHHCCCCHHHH		24.3728857561
223UbiquitinationMELFPANKQSVEHFT
HHHCCCCHHHHHHHH		46.1621890473
223AcetylationMELFPANKQSVEHFT
HHHCCCCHHHHHHHH		46.1625953088
223MalonylationMELFPANKQSVEHFT
HHHCCCCHHHHHHHH		46.1626320211
223UbiquitinationMELFPANKQSVEHFT
HHHCCCCHHHHHHHH		46.16-
223 (in isoform 1)Ubiquitination-46.1621890473
223 (in isoform 2)Ubiquitination-46.1621890473
225PhosphorylationLFPANKQSVEHFTKY
HCCCCHHHHHHHHHH		30.9627251275
227UbiquitinationPANKQSVEHFTKYFT
CCCHHHHHHHHHHHH		38.2321890473
229UbiquitinationNKQSVEHFTKYFTEA
CHHHHHHHHHHHHHH		3.8921890473
229 (in isoform 3)Ubiquitination-3.89-
230PhosphorylationKQSVEHFTKYFTEAG
HHHHHHHHHHHHHHH		27.0924719451
231AcetylationQSVEHFTKYFTEAGL
HHHHHHHHHHHHHHH		37.1127452117
231UbiquitinationQSVEHFTKYFTEAGL
HHHHHHHHHHHHHHH		37.1121890473
231 (in isoform 1)Ubiquitination-37.1121890473
231 (in isoform 2)Ubiquitination-37.1121890473
232PhosphorylationSVEHFTKYFTEAGLK
HHHHHHHHHHHHHHH		16.8129759185
234PhosphorylationEHFTKYFTEAGLKEL
HHHHHHHHHHHHHHH		23.1029759185
235UbiquitinationHFTKYFTEAGLKELS
HHHHHHHHHHHHHHH		30.7321890473
237 (in isoform 3)Phosphorylation-30.9327251275
239UbiquitinationYFTEAGLKELSEYVR
HHHHHHHHHHHHHHH		56.5421890473
239 (in isoform 1)Ubiquitination-56.5421890473
239 (in isoform 2)Ubiquitination-56.5421890473
242PhosphorylationEAGLKELSEYVRNQQ
HHHHHHHHHHHHHHH		28.1528857561
242 (in isoform 3)Phosphorylation-28.1524719451
243UbiquitinationAGLKELSEYVRNQQT
HHHHHHHHHHHHHHC		61.7521890473
244PhosphorylationGLKELSEYVRNQQTI
HHHHHHHHHHHHHCH		11.00-
255UbiquitinationQQTIGARKELQKELQ
HHCHHHHHHHHHHHH		63.3421890473
255UbiquitinationQQTIGARKELQKELQ
HHCHHHHHHHHHHHH		63.34-
255 (in isoform 3)Malonylation-63.3426320211
255 (in isoform 3)Ubiquitination-63.34-
257 (in isoform 3)Phosphorylation-11.2027251275
259AcetylationGARKELQKELQEQMS
HHHHHHHHHHHHHHH		73.3723236377
259UbiquitinationGARKELQKELQEQMS
HHHHHHHHHHHHHHH		73.3721890473
259 (in isoform 1)Ubiquitination-73.3721890473
259 (in isoform 2)Ubiquitination-73.3721890473
262 (in isoform 3)Phosphorylation-39.7124719451
263UbiquitinationELQKELQEQMSRGDP
HHHHHHHHHHHCCCC		61.9621890473
263UbiquitinationELQKELQEQMSRGDP
HHHHHHHHHHHCCCC		61.9621890473
271UbiquitinationQMSRGDPFKDIILYV
HHHCCCCHHHHHHHH		15.3421890473
271 (in isoform 3)Ubiquitination-15.34-
272AcetylationMSRGDPFKDIILYVK
HHCCCCHHHHHHHHH		54.1027452117
272UbiquitinationMSRGDPFKDIILYVK
HHCCCCHHHHHHHHH		54.1021890473
272 (in isoform 1)Ubiquitination-54.1021890473
272 (in isoform 2)Ubiquitination-54.1021890473
276UbiquitinationDPFKDIILYVKEEMK
CCHHHHHHHHHHHHH		4.0321890473
277PhosphorylationPFKDIILYVKEEMKK
CHHHHHHHHHHHHHH		10.0828152594
287 (in isoform 3)Ubiquitination-5.97-
291UbiquitinationKNNIPEPVVIGIVWS
HCCCCCCEEEEEHHH		4.7021890473
291 (in isoform 3)Ubiquitination-4.70-
298PhosphorylationVVIGIVWSSVMSTVE
EEEEEHHHHHHHHCC		11.3622468782
304UbiquitinationWSSVMSTVEWNKKEE
HHHHHHHCCCCHHHH		6.6821890473
304 (in isoform 3)Ubiquitination-6.68-
309UbiquitinationSTVEWNKKEELVAEQ
HHCCCCHHHHHHHHH		53.8921906983
309 (in isoform 1)Ubiquitination-53.8921890473
313 (in isoform 2)Ubiquitination-6.6121890473
322UbiquitinationEQAIKHLKQYSPLLA
HHHHHHHHHHCHHHH		47.08-
333PhosphorylationPLLAAFTTQGQSELT
HHHHHHHCCCCCHHH		25.0127067055
333 (in isoform 2)Ubiquitination-25.0121890473
337PhosphorylationAFTTQGQSELTLLLK
HHHCCCCCHHHHHHH		41.2027067055
340PhosphorylationTQGQSELTLLLKIQE
CCCCCHHHHHHHHHH		16.0027067055
357AcetylationYDNIHFMKAFQKIVV
CCCHHHHHHHHHHHH		45.1427452117
357UbiquitinationYDNIHFMKAFQKIVV
CCCHHHHHHHHHHHH		45.14-
368SumoylationKIVVLFYKAEVLSEE
HHHHHHHHHHCCCCC		30.6428112733
368UbiquitinationKIVVLFYKAEVLSEE
HHHHHHHHHHCCCCC		30.64-
379AcetylationLSEEPILKWYKDAHV
CCCCCCHHHHHHHHH		49.5527452117
379UbiquitinationLSEEPILKWYKDAHV
CCCCCCHHHHHHHHH		49.5521906983
379 (in isoform 1)Ubiquitination-49.5521890473
382UbiquitinationEPILKWYKDAHVAKG
CCCHHHHHHHHHHCC		47.53-
383UbiquitinationPILKWYKDAHVAKGK
CCHHHHHHHHHHCCC		26.6421890473
390AcetylationDAHVAKGKSVFLEQM
HHHHHCCCHHHHHHH		42.6226051181
390MalonylationDAHVAKGKSVFLEQM
HHHHHCCCHHHHHHH		42.6226320211
390UbiquitinationDAHVAKGKSVFLEQM
HHHHHCCCHHHHHHH		42.62-
391PhosphorylationAHVAKGKSVFLEQMK
HHHHCCCHHHHHHHH		27.1123403867
398AcetylationSVFLEQMKKFVEWLK
HHHHHHHHHHHHHHH		42.6325953088
399AcetylationVFLEQMKKFVEWLKN
HHHHHHHHHHHHHHC		49.6625953088
399UbiquitinationVFLEQMKKFVEWLKN
HHHHHHHHHHHHHHC		49.662189047
399 (in isoform 1)Ubiquitination-49.6621890473
403UbiquitinationQMKKFVEWLKNAEEE
HHHHHHHHHHCHHHH		13.8221890473
411UbiquitinationLKNAEEESESEAEEG
HHCHHHHHHHHHHCC		50.1021890473
411PhosphorylationLKNAEEESESEAEEG
HHCHHHHHHHHHHCC		50.1026846344
413PhosphorylationNAEEESESEAEEGD-
CHHHHHHHHHHCCC-		51.9226846344
422 (in isoform 3)Malonylation-26320211
422 (in isoform 3)Ubiquitination--
423 (in isoform 3)Phosphorylation-24719451
430 (in isoform 3)Malonylation-32601280
431Ubiquitination-------------------
-------------------		21890473
431 (in isoform 3)Ubiquitination--
443 (in isoform 3)Phosphorylation-24719451
445 (in isoform 3)Phosphorylation-24719451
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 BZW1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BZW1_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 BZW1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BZW2_HUMANBZW2physical
17353931
PPIP1_HUMANPSTPIP1physical
17353931
ERD21_HUMANKDELR1physical
17353931
EDEM1_HUMANEDEM1physical
17353931
CMYA5_HUMANCMYA5physical
17353931
DCTN1_HUMANDCTN1physical
17353931
MAGI1_HUMANMAGI1physical
17353931
PREX1_HUMANPREX1physical
17353931
RA1L2_HUMANHNRNPA1L2physical
22939629
GNAI3_HUMANGNAI3physical
22863883
TXND5_HUMANTXNDC5physical
22863883
BZW2_HUMANBZW2physical
26186194
PRP31_HUMANPRPF31physical
26186194
ENPP1_HUMANENPP1physical
26186194
SCPDL_HUMANSCCPDHphysical
26186194
RN138_HUMANRNF138physical
26186194
TMM43_HUMANTMEM43physical
26186194
ARHL2_HUMANADPRHL2physical
26344197
IF5_HUMANEIF5physical
26344197
ERF1_HUMANETF1physical
26344197
ZMYM3_HUMANZMYM3physical
26344197
BZW2_HUMANBZW2physical
28514442
RN138_HUMANRNF138physical
28514442
SCPDL_HUMANSCCPDHphysical
28514442
ENPP1_HUMANENPP1physical
28514442
TMM43_HUMANTMEM43physical
28514442
STOM_HUMANSTOMphysical
27173435
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 BZW1_HUMAN

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Related Literatures of Post-Translational Modification
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-411 AND SER-413, 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-411 AND SER-413, ANDMASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-413, ANDMASS SPECTROMETRY.
"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-411 AND SER-413, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND MASSSPECTROMETRY.
"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-411 AND SER-413, ANDMASS SPECTROMETRY.

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