ZN33A_HUMAN - dbPTM
ZN33A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN33A_HUMAN
UniProt AC Q06730
Protein Name Zinc finger protein 33A
Gene Name ZNF33A
Organism Homo sapiens (Human).
Sequence Length 810
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MNKVEQKSQESVSFKDVTVGFTQEEWQHLDPSQRALYRDVMLENYSNLVSVGYCVHKPEVIFRLQQGEEPWKQEEEFPSQSFPVWTADHLKERSQENQSKHLWEVVFINNEMLTKEQGDVIGIPFNVDVSSFPSRKMFCQCDSCGMSFNTVSELVISKINYLGKKSDEFNACGKLLLNIKHDETHTQEKNEVLKNRNTLSHHEETLQHEKIQTLEHNFEYSICQETLLEKAVFNTQKRENAEENNCDYNEFGRTLCDSSSLLFHQISPSRDNHYEFSDCEKFLCVKSTLSKPHGVSMKHYDCGESGNNFRRKLCLSHLQKGDKGEKHFECNECGKAFWEKSHLTRHQRVHTGQKPFQCNECEKAFWDKSNLTKHQRSHTGEKPFECNECGKAFSHKSALTLHQRTHTGEKPYQCNACGKTFCQKSDLTKHQRTHTGLKPYECYECGKSFRVTSHLKVHQRTHTGEKPFECLECGKSFSEKSNLTQHQRIHIGDKSYECNACGKTFYHKSLLTRHQIIHTGWKPYECYECGKTFCLKSDLTVHQRTHTGQKPFACPECGKFFSHKSTLSQHYRTHTGEKPYECHECGKIFYNKSYLTKHNRTHTGEKPYECNECGKAFYQKSQLTQHQRIHIGEKPYKCNECGKAFCHKSALIVHQRTHTQEKPYKCNECGKSFCVKSGLIFHERKHTGEKPYECNECGKFFRHKSSLTVHHRAHTGEKSCQCNECGKIFYRKSELAQHQRSHTGEKPYECNTCRKTFSQKSNLIVHQRRHIGENLMNEMDIRNFQPQVSLHNASEYSHCGESPDDILNVQ
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
3Ubiquitination-----MNKVEQKSQE
-----CCHHCHHHHC
45.94-
7Ubiquitination-MNKVEQKSQESVSF
-CCHHCHHHHCCCCC
40.37-
8PhosphorylationMNKVEQKSQESVSFK
CCHHCHHHHCCCCCC
38.5829083192
11PhosphorylationVEQKSQESVSFKDVT
HCHHHHCCCCCCCEE
18.5429083192
13PhosphorylationQKSQESVSFKDVTVG
HHHHCCCCCCCEEEC
35.5424719451
15AcetylationSQESVSFKDVTVGFT
HHCCCCCCCEEECCC
43.7312437799
18PhosphorylationSVSFKDVTVGFTQEE
CCCCCCEEECCCHHH
25.6625002506
22PhosphorylationKDVTVGFTQEEWQHL
CCEEECCCHHHHHHC
29.1925002506
32PhosphorylationEWQHLDPSQRALYRD
HHHHCCHHHHHHHHH
31.7825002506
165UbiquitinationKINYLGKKSDEFNAC
HHHHCCCCCHHCCHH
62.43-
166PhosphorylationINYLGKKSDEFNACG
HHHCCCCCHHCCHHH
45.9528555341
172UbiquitinationKSDEFNACGKLLLNI
CCHHCCHHHHHHHHC
5.32-
180SumoylationGKLLLNIKHDETHTQ
HHHHHHCCCCCCCHH
43.88-
180SumoylationGKLLLNIKHDETHTQ
HHHHHHCCCCCCCHH
43.8828112733
180UbiquitinationGKLLLNIKHDETHTQ
HHHHHHCCCCCCCHH
43.88-
184PhosphorylationLNIKHDETHTQEKNE
HHCCCCCCCHHHHHH
35.9630624053
186PhosphorylationIKHDETHTQEKNEVL
CCCCCCCHHHHHHHH
45.9330624053
189UbiquitinationDETHTQEKNEVLKNR
CCCCHHHHHHHHHCC
48.90-
194UbiquitinationQEKNEVLKNRNTLSH
HHHHHHHHCCCCCCC
60.06-
196UbiquitinationKNEVLKNRNTLSHHE
HHHHHHCCCCCCCHH
35.60-
201UbiquitinationKNRNTLSHHEETLQH
HCCCCCCCHHHHHHH
35.18-
237SumoylationKAVFNTQKRENAEEN
HHHHCHHHHHCHHHC
60.69-
237SumoylationKAVFNTQKRENAEEN
HHHHCHHHHHCHHHC
60.6928112733
237UbiquitinationKAVFNTQKRENAEEN
HHHHCHHHHHCHHHC
60.69-
244UbiquitinationKRENAEENNCDYNEF
HHHCHHHCCCCHHHH
46.03-
258PhosphorylationFGRTLCDSSSLLFHQ
HHHHHHCHHHCEEEE
22.3423312004
259PhosphorylationGRTLCDSSSLLFHQI
HHHHHCHHHCEEEEC
16.2623312004
260PhosphorylationRTLCDSSSLLFHQIS
HHHHCHHHCEEEECC
32.8023312004
267PhosphorylationSLLFHQISPSRDNHY
HCEEEECCCCCCCCC
15.3923401153
268PhosphorylationLLFHQISPSRDNHYE
CEEEECCCCCCCCCC
34.7024719451
269PhosphorylationLFHQISPSRDNHYEF
EEEECCCCCCCCCCC
45.5425849741
281UbiquitinationYEFSDCEKFLCVKST
CCCCCCCEEEEEECC
50.39-
282PhosphorylationEFSDCEKFLCVKSTL
CCCCCCEEEEEECCC
2.7427251275
286UbiquitinationCEKFLCVKSTLSKPH
CCEEEEEECCCCCCC
36.40-
289PhosphorylationFLCVKSTLSKPHGVS
EEEEECCCCCCCCCC
8.8227251275
312UbiquitinationSGNNFRRKLCLSHLQ
CCCCHHHHHHHHHHH
39.02-
312SumoylationSGNNFRRKLCLSHLQ
CCCCHHHHHHHHHHH
39.0228112733
335UbiquitinationFECNECGKAFWEKSH
EEECHHHHHHHHHHC
52.66-
340SumoylationCGKAFWEKSHLTRHQ
HHHHHHHHHCCCCHH
33.50-
340SumoylationCGKAFWEKSHLTRHQ
HHHHHHHHHCCCCHH
33.50-
340UbiquitinationCGKAFWEKSHLTRHQ
HHHHHHHHHCCCCHH
33.50-
342UbiquitinationKAFWEKSHLTRHQRV
HHHHHHHCCCCHHHH
42.14-
347UbiquitinationKSHLTRHQRVHTGQK
HHCCCCHHHHHCCCC
45.89-
351PhosphorylationTRHQRVHTGQKPFQC
CCHHHHHCCCCCCCC
38.1521712546
354SumoylationQRVHTGQKPFQCNEC
HHHHCCCCCCCCCHH
49.50-
354SumoylationQRVHTGQKPFQCNEC
HHHHCCCCCCCCCHH
49.50-
354UbiquitinationQRVHTGQKPFQCNEC
HHHHCCCCCCCCCHH
49.50-
363UbiquitinationFQCNECEKAFWDKSN
CCCCHHHHHHCCCCC
61.62-
368SumoylationCEKAFWDKSNLTKHQ
HHHHHCCCCCCCCCC
31.66-
368SumoylationCEKAFWDKSNLTKHQ
HHHHHCCCCCCCCCC
31.66-
368UbiquitinationCEKAFWDKSNLTKHQ
HHHHHCCCCCCCCCC
31.66-
370UbiquitinationKAFWDKSNLTKHQRS
HHHCCCCCCCCCCCC
58.43-
375UbiquitinationKSNLTKHQRSHTGEK
CCCCCCCCCCCCCCC
50.56-
382UbiquitinationQRSHTGEKPFECNEC
CCCCCCCCCEECCCC
57.25-
382AcetylationQRSHTGEKPFECNEC
CCCCCCCCCEECCCC
57.2520167786
389UbiquitinationKPFECNECGKAFSHK
CCEECCCCCCCCCCC
4.16-
405PhosphorylationALTLHQRTHTGEKPY
CEEEECCCCCCCCCE
19.74-
407PhosphorylationTLHQRTHTGEKPYQC
EEECCCCCCCCCEEC
46.56-
410UbiquitinationQRTHTGEKPYQCNAC
CCCCCCCCCEECCCC
50.82-
417UbiquitinationKPYQCNACGKTFCQK
CCEECCCCCCEEECH
3.41-
424UbiquitinationCGKTFCQKSDLTKHQ
CCCEEECHHCCCCCC
47.31-
425PhosphorylationGKTFCQKSDLTKHQR
CCEEECHHCCCCCCC
16.3929978859
428PhosphorylationFCQKSDLTKHQRTHT
EECHHCCCCCCCCCC
31.3229978859
431UbiquitinationKSDLTKHQRTHTGLK
HHCCCCCCCCCCCCC
54.23-
433PhosphorylationDLTKHQRTHTGLKPY
CCCCCCCCCCCCCCE
19.7429978859
435PhosphorylationTKHQRTHTGLKPYEC
CCCCCCCCCCCCEEE
43.5329978859
448PhosphorylationECYECGKSFRVTSHL
EEEECCCEEEEEEEE
11.99-
456UbiquitinationFRVTSHLKVHQRTHT
EEEEEEEEEEECCCC
32.04-
456SumoylationFRVTSHLKVHQRTHT
EEEEEEEEEEECCCC
32.0428112733
461PhosphorylationHLKVHQRTHTGEKPF
EEEEEECCCCCCCCE
19.74-
463PhosphorylationKVHQRTHTGEKPFEC
EEEECCCCCCCCEEE
46.56-
466UbiquitinationQRTHTGEKPFECLEC
ECCCCCCCCEEEECC
57.25-
473UbiquitinationKPFECLECGKSFSEK
CCEEEECCCCCCCCC
5.55-
480SumoylationCGKSFSEKSNLTQHQ
CCCCCCCCCCCCCCC
43.37-
480SumoylationCGKSFSEKSNLTQHQ
CCCCCCCCCCCCCCC
43.37-
480UbiquitinationCGKSFSEKSNLTQHQ
CCCCCCCCCCCCCCC
43.37-
508SumoylationCGKTFYHKSLLTRHQ
CCCCEECHHHHHHHH
31.27-
508SumoylationCGKTFYHKSLLTRHQ
CCCCEECHHHHHHHH
31.27-
509PhosphorylationGKTFYHKSLLTRHQI
CCCEECHHHHHHHHE
18.4624719451
510PhosphorylationKTFYHKSLLTRHQII
CCEECHHHHHHHHEE
7.2624719451
536SumoylationCGKTFCLKSDLTVHQ
CCCEEEEECCCEEEE
43.00-
536SumoylationCGKTFCLKSDLTVHQ
CCCEEEEECCCEEEE
43.00-
545PhosphorylationDLTVHQRTHTGQKPF
CCEEEECCCCCCCCC
19.7428258704
573PhosphorylationTLSQHYRTHTGEKPY
HHHHHHHHCCCCCCE
19.34-
575PhosphorylationSQHYRTHTGEKPYEC
HHHHHHCCCCCCEEE
46.56-
590PhosphorylationHECGKIFYNKSYLTK
CCCCCEEECHHHHHC
25.75-
592SumoylationCGKIFYNKSYLTKHN
CCCEEECHHHHHCCC
29.15-
592SumoylationCGKIFYNKSYLTKHN
CCCEEECHHHHHCCC
29.15-
594PhosphorylationKIFYNKSYLTKHNRT
CEEECHHHHHCCCCC
21.72-
601PhosphorylationYLTKHNRTHTGEKPY
HHHCCCCCCCCCCCC
29.1628348404
603PhosphorylationTKHNRTHTGEKPYEC
HCCCCCCCCCCCCCC
46.5629496963
606UbiquitinationNRTHTGEKPYECNEC
CCCCCCCCCCCCCHH
55.00-
620SumoylationCGKAFYQKSQLTQHQ
HHHHHHHHHCCCCCC
28.88-
620SumoylationCGKAFYQKSQLTQHQ
HHHHHHHHHCCCCCC
28.88-
620UbiquitinationCGKAFYQKSQLTQHQ
HHHHHHHHHCCCCCC
28.88-
627UbiquitinationKSQLTQHQRIHIGEK
HHCCCCCCCEECCCC
35.88-
634UbiquitinationQRIHIGEKPYKCNEC
CCEECCCCCCCCCCC
48.73-
637SumoylationHIGEKPYKCNECGKA
ECCCCCCCCCCCCCC
38.83-
637SumoylationHIGEKPYKCNECGKA
ECCCCCCCCCCCCCC
38.83-
665SumoylationHTQEKPYKCNECGKS
CCCCCCEECCCCCCE
38.83-
665SumoylationHTQEKPYKCNECGKS
CCCCCCEECCCCCCE
38.83-
672PhosphorylationKCNECGKSFCVKSGL
ECCCCCCEEEEECCC
14.7930108239
676SumoylationCGKSFCVKSGLIFHE
CCCEEEEECCCEEEC
39.73-
676SumoylationCGKSFCVKSGLIFHE
CCCEEEEECCCEEEC
39.7328112733
687PhosphorylationIFHERKHTGEKPYEC
EEECCCCCCCCCEEC
50.5023532336
690UbiquitinationERKHTGEKPYECNEC
CCCCCCCCCEECCCC
55.00-
699SumoylationYECNECGKFFRHKSS
EECCCCCCEEECCCC
53.65-
699UbiquitinationYECNECGKFFRHKSS
EECCCCCCEEECCCC
53.65-
699SumoylationYECNECGKFFRHKSS
EECCCCCCEEECCCC
53.65-
727UbiquitinationCQCNECGKIFYRKSE
CCCCCCCCEEEEHHH
41.10-
732SumoylationCGKIFYRKSELAQHQ
CCCEEEEHHHHHHHH
36.5828112733
734UbiquitinationKIFYRKSELAQHQRS
CEEEEHHHHHHHHHH
51.68-
760SumoylationCRKTFSQKSNLIVHQ
CCCCCCCCCCEEEEE
39.86-
760SumoylationCRKTFSQKSNLIVHQ
CCCCCCCCCCEEEEE
39.86-

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 ZN33A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN33A_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 ZN33A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K20_HUMANZAKphysical
12535642

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 ZN33A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND MASSSPECTROMETRY.

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