ZN165_HUMAN - dbPTM
ZN165_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN165_HUMAN
UniProt AC P49910
Protein Name Zinc finger protein 165
Gene Name ZNF165
Organism Homo sapiens (Human).
Sequence Length 485
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MATEPKKAAAQNSPEDEGLLIVKIEEEEFIHGQDTCLQRSELLKQELCRQLFRQFCYQDSPGPREALSRLRELCCQWLKPEIHTKEQILELLVLEQFLTILPGDLQAWVHEHYPESGEEAVTILEDLERGTDEAVLQVQAHEHGQEIFQKKVSPPGPALNVKLQPVETKAHFDSSEPQLLWDCDNESENSRSMPKLEIFEKIESQRIISGRISGYISEASGESQDICKSAGRVKRQWEKESGESQRLSSAQDEGFGKILTHKNTVRGEIISHDGCERRLNLNSNEFTHQKSCKHGTCDQSFKWNSDFINHQIIYAGEKNHQYGKSFKSPKLAKHAAVFSGDKTHQCNECGKAFRHSSKLARHQRIHTGERCYECNECGKSFAESSDLTRHRRIHTGERPFGCKECGRAFNLNSHLIRHQRIHTREKPYECSECGKTFRVSSHLIRHFRIHTGEKPYECSECGRAFSQSSNLSQHQRIHMRENLLM
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
13PhosphorylationKKAAAQNSPEDEGLL
HHHHHCCCCCCCCEE
20.0021815630
23SumoylationDEGLLIVKIEEEEFI
CCCEEEEEECHHHCC
37.0928112733
35PhosphorylationEFIHGQDTCLQRSEL
HCCCCCCCHHHHHHH
13.7627251275
40PhosphorylationQDTCLQRSELLKQEL
CCCHHHHHHHHHHHH
21.4527251275
68PhosphorylationPGPREALSRLRELCC
CCHHHHHHHHHHHHH
36.00-
153PhosphorylationEIFQKKVSPPGPALN
HHHHCCCCCCCCCCE
33.9725849741
162SumoylationPGPALNVKLQPVETK
CCCCCEEEEEECEEE
40.0928112733
195SumoylationENSRSMPKLEIFEKI
CCCCCCCHHHHHHHH
50.5428112733
209PhosphorylationIESQRIISGRISGYI
HHHCCEEECCHHHEE
21.4622210691
241PhosphorylationKRQWEKESGESQRLS
HHHHHHHCCCCCCHH
59.95-
244PhosphorylationWEKESGESQRLSSAQ
HHHHCCCCCCHHCHH
24.91-
248PhosphorylationSGESQRLSSAQDEGF
CCCCCCHHCHHCCCC
26.30-
324UbiquitinationEKNHQYGKSFKSPKL
CCCCCCCCCCCCHHH
48.03-
327UbiquitinationHQYGKSFKSPKLAKH
CCCCCCCCCHHHHHH
73.30-
328PhosphorylationQYGKSFKSPKLAKHA
CCCCCCCCHHHHHHE
25.8424719451
330UbiquitinationGKSFKSPKLAKHAAV
CCCCCCHHHHHHEEE
69.07-
385PhosphorylationGKSFAESSDLTRHRR
CCCHHHCCCCCCCCC
28.3023532336
413PhosphorylationGRAFNLNSHLIRHQR
CCCCCCCHHHHHCCC
23.8824719451
451PhosphorylationIRHFRIHTGEKPYEC
HHCEEEECCCCCEEC
44.6728111955
456PhosphorylationIHTGEKPYECSECGR
EECCCCCEECCHHHC
40.41-

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 ZN165_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN165_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 ZN165_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELOA2_HUMANTCEB3Bphysical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
KAT7_HUMANKAT7physical
16189514
CC130_HUMANCCDC130physical
16189514
ZN446_HUMANZNF446physical
16189514
KR412_HUMANKRTAP4-12physical
16189514
F124A_HUMANFAM124Aphysical
16189514
SCND1_HUMANSCAND1physical
16189514
PDLI7_HUMANPDLIM7physical
16189514
ZN250_HUMANZNF250physical
16189514
ZNF24_HUMANZNF24physical
10567577
ZKSC8_HUMANZKSCAN8physical
10567577
SUV91_HUMANSUV39H1physical
23455924
SAHH2_HUMANAHCYL1physical
25416956
TRIM1_HUMANMID2physical
25416956
ZN446_HUMANZNF446physical
25416956
GPT2L_HUMANGPATCH2Lphysical
25416956
K1C40_HUMANKRT40physical
25416956
F124A_HUMANFAM124Aphysical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR103_HUMANKRTAP10-3physical
25416956

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN165_HUMAN

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Related Literatures of Post-Translational Modification

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