ZN468_HUMAN - dbPTM
ZN468_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN468_HUMAN
UniProt AC Q5VIY5
Protein Name Zinc finger protein 468
Gene Name ZNF468
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MALPQGLLTFRDVAIEFSQEEWKCLDPAQRTLYRDVMLENYRNLVSLDISSKCMLKTLSSTGQGNTEVIHTGTLHRQASHHIGEFCFHEIEKDIHGFEFQWKEDETNGHAAPMTEIKELAGSTGQHDQRHAGNKRIKDQLGSSFHLHLPEPHIFQSEGKIGNQVEKSINNASSVSTSQRICCRPKTHISNKYGNNSLHSSLLTQKWEVHMREKSFECIQSFKSFNCSSLLKKHQIIHLEEKQCKCDVCGKVFNQKRYLACHRRCHTGEKPYKCNECGKTFGHNSSLFIHKALHTGEKPYECEECDKVFSRKSHLERHKRIHTGEKPYKCKVCDEAFAYNSYLAKHTILHTGEKPYTCNECGKVFNRLSTLARHHRLHTGEKPYKCEECDKVFSRKSHLERHRRIHSGEKPYKCEECCKVFSRKSNLERHRRIHTGEKPYKCKVCDKAFQRDSHLAQHQRVHTGEKPYKCNECGKTFGQTSSLIIHRRLHTGEKPYKCNECGKTFSQMSSLVYHHRLHSGEKP
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
18PhosphorylationRDVAIEFSQEEWKCL
HHHHHCCCHHHHHHC
24.7227251275
23UbiquitinationEFSQEEWKCLDPAQR
CCCHHHHHHCCHHHH
28.35-
41PhosphorylationRDVMLENYRNLVSLD
HHHHHHHHHHCEECC
7.4822210691
46PhosphorylationENYRNLVSLDISSKC
HHHHHCEECCCCCCH
24.4022210691
79PhosphorylationGTLHRQASHHIGEFC
CEECCCCCHHHHCHH
13.78-
113 (in isoform 2)Ubiquitination-4.5021890473
142PhosphorylationRIKDQLGSSFHLHLP
HHHHHHCCCEEEECC
38.1228555341
166UbiquitinationKIGNQVEKSINNASS
CHHHHHHHHHHCCCC
58.75-
166 (in isoform 1)Ubiquitination-58.7521890473
167PhosphorylationIGNQVEKSINNASSV
HHHHHHHHHHCCCCC
19.6228555341
186PhosphorylationRICCRPKTHISNKYG
EEEECCCCCCCCCCC
27.4226552605
189PhosphorylationCRPKTHISNKYGNNS
ECCCCCCCCCCCCCC
21.4726552605
191UbiquitinationPKTHISNKYGNNSLH
CCCCCCCCCCCCCHH
47.98-
192PhosphorylationKTHISNKYGNNSLHS
CCCCCCCCCCCCHHH
29.3626552605
196PhosphorylationSNKYGNNSLHSSLLT
CCCCCCCCHHHHHHH
31.3026552605
199PhosphorylationYGNNSLHSSLLTQKW
CCCCCHHHHHHHHCC
28.1626552605
200PhosphorylationGNNSLHSSLLTQKWE
CCCCHHHHHHHHCCE
19.3626552605
203PhosphorylationSLHSSLLTQKWEVHM
CHHHHHHHHCCEEEE
33.1426552605
223PhosphorylationECIQSFKSFNCSSLL
HHHHHHHCCCHHHHH
21.4929970186
228PhosphorylationFKSFNCSSLLKKHQI
HHCCCHHHHHHHHCE
39.6624719451
250UbiquitinationCKCDVCGKVFNQKRY
CCCCCCHHHHCCHHH
38.23-
272SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
272UbiquitinationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
272SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
297UbiquitinationKALHTGEKPYECEEC
HHHCCCCCCCCCHHH
55.00-
322PhosphorylationERHKRIHTGEKPYKC
HHHHCCCCCCCCCCC
44.6729496963
328 (in isoform 2)Ubiquitination-35.7921890473
328UbiquitinationHTGEKPYKCKVCDEA
CCCCCCCCCCCCCCH
35.7921890473
328UbiquitinationHTGEKPYKCKVCDEA
CCCCCCCCCCCCCCH
35.7921890473
330UbiquitinationGEKPYKCKVCDEAFA
CCCCCCCCCCCCHHH
41.57-
350PhosphorylationAKHTILHTGEKPYTC
HHCCEEECCCCCEEC
43.5221857030
353UbiquitinationTILHTGEKPYTCNEC
CEEECCCCCEECCHH
44.67-
368PhosphorylationGKVFNRLSTLARHHR
HHHHHHHHHHHHHCC
20.3824945436
378PhosphorylationARHHRLHTGEKPYKC
HHHCCCCCCCCCCCC
52.1827422710
381SumoylationHRLHTGEKPYKCEEC
CCCCCCCCCCCCHHC
55.80-
381SumoylationHRLHTGEKPYKCEEC
CCCCCCCCCCCCHHC
55.80-
381UbiquitinationHRLHTGEKPYKCEEC
CCCCCCCCCCCCHHC
55.8021890473
381 (in isoform 1)Ubiquitination-55.8021890473
384SumoylationHTGEKPYKCEECDKV
CCCCCCCCCHHCHHH
43.63-
384SumoylationHTGEKPYKCEECDKV
CCCCCCCCCHHCHHH
43.63-
384UbiquitinationHTGEKPYKCEECDKV
CCCCCCCCCHHCHHH
43.63-
400UbiquitinationSRKSHLERHRRIHSG
CCHHHHHHHHHHCCC
34.6721890473
406PhosphorylationERHRRIHSGEKPYKC
HHHHHHCCCCCCCCH
46.4029496963
412UbiquitinationHSGEKPYKCEECCKV
CCCCCCCCHHHHHHH
43.63-
434PhosphorylationERHRRIHTGEKPYKC
HHHHHCCCCCCCCCC
44.6729496963
439PhosphorylationIHTGEKPYKCKVCDK
CCCCCCCCCCCCCCH
39.83-
440UbiquitinationHTGEKPYKCKVCDKA
CCCCCCCCCCCCCHH
35.7921890473
462PhosphorylationAQHQRVHTGEKPYKC
HHHCCCCCCCCCEEC
44.1529496963
465SumoylationQRVHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
465UbiquitinationQRVHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
465SumoylationQRVHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
468SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
468SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
468UbiquitinationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
490PhosphorylationIIHRRLHTGEKPYKC
EEEEECCCCCCCEEC
52.1827422710
493SumoylationRRLHTGEKPYKCNEC
EECCCCCCCEECCCC
55.80-
493UbiquitinationRRLHTGEKPYKCNEC
EECCCCCCCEECCCC
55.8021890473
493SumoylationRRLHTGEKPYKCNEC
EECCCCCCCEECCCC
55.80-
495PhosphorylationLHTGEKPYKCNECGK
CCCCCCCEECCCCCC
38.96-
496SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
496UbiquitinationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
496SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
512UbiquitinationSQMSSLVYHHRLHSG
HHHHHHHHHHHCCCC
9.3721890473
518PhosphorylationVYHHRLHSGEKP---
HHHHHCCCCCCC---
53.92-

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 ZN468_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN468_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 ZN468_HUMAN !!

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

Oops, there are no PPI records of ZN468_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN468_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP