ZER1_HUMAN - dbPTM
ZER1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZER1_HUMAN
UniProt AC Q7Z7L7
Protein Name Protein zer-1 homolog
Gene Name ZER1
Organism Homo sapiens (Human).
Sequence Length 766
Subcellular Localization
Protein Description Probably acts as target recruitment subunit in the E3 ubiquitin ligase complex ZER1-CUL2-Elongin BC..
Protein Sequence MASDTPESLMALCTDFCLRNLDGTLGYLLDKETLRLHPDIFLPSEICDRLVNEYVELVNAACNFEPHESFFSLFSDPRSTRLTRIHLREDLVQDQDLEAIRKQDLVELYLTNCEKLSAKSLQTLRSFSHTLVSLSLFGCTNIFYEEENPGGCEDEYLVNPTCQVLVKDFTFEGFSRLRFLNLGRMIDWVPVESLLRPLNSLAALDLSGIQTSDAAFLTQWKDSLVSLVLYNMDLSDDHIRVIVQLHKLRHLDISRDRLSSYYKFKLTREVLSLFVQKLGNLMSLDISGHMILENCSISKMEEEAGQTSIEPSKSSIIPFRALKRPLQFLGLFENSLCRLTHIPAYKVSGDKNEEQVLNAIEAYTEHRPEITSRAINLLFDIARIERCNQLLRALKLVITALKCHKYDRNIQVTGSAALFYLTNSEYRSEQSVKLRRQVIQVVLNGMESYQEVTVQRNCCLTLCNFSIPEELEFQYRRVNELLLSILNPTRQDESIQRIAVHLCNALVCQVDNDHKEAVGKMGFVVTMLKLIQKKLLDKTCDQVMEFSWSALWNITDETPDNCEMFLNFNGMKLFLDCLKEFPEKQELHRNMLGLLGNVAEVKELRPQLMTSQFISVFSNLLESKADGIEVSYNACGVLSHIMFDGPEAWGVCEPQREEVEERMWAAIQSWDINSRRNINYRSFEPILRLLPQGISPVSQHWATWALYNLVSVYPDKYCPLLIKEGGMPLLRDIIKMATARQETKEMARKVIEHCSNFKEENMDTSR
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
2Acetylation------MASDTPESL
------CCCCCHHHH
19.0022814378
24PhosphorylationCLRNLDGTLGYLLDK
HHHCCCCCHHHHCCH
19.3722199227
31UbiquitinationTLGYLLDKETLRLHP
CHHHHCCHHHHHCCC
53.2021906983
102UbiquitinationQDLEAIRKQDLVELY
CCHHHHHHHHHHHHH
41.89-
115UbiquitinationLYLTNCEKLSAKSLQ
HHHHCHHHCCHHHHH
50.36-
119UbiquitinationNCEKLSAKSLQTLRS
CHHHCCHHHHHHHHH
48.61-
230PhosphorylationSLVSLVLYNMDLSDD
HHHHHEEECCCCCHH
10.85-
254PhosphorylationKLRHLDISRDRLSSY
HHCCCCCCHHHHHHH
28.0026270265
260PhosphorylationISRDRLSSYYKFKLT
CCHHHHHHHHHHHHH
36.7522461510
261PhosphorylationSRDRLSSYYKFKLTR
CHHHHHHHHHHHHHH
13.8022461510
263UbiquitinationDRLSSYYKFKLTREV
HHHHHHHHHHHHHHH
27.99-
307PhosphorylationMEEEAGQTSIEPSKS
HHHHHCCCCCCCCCC
30.6523403867
308PhosphorylationEEEAGQTSIEPSKSS
HHHHCCCCCCCCCCC
19.6423403867
312PhosphorylationGQTSIEPSKSSIIPF
CCCCCCCCCCCCCCH
32.1723403867
313UbiquitinationQTSIEPSKSSIIPFR
CCCCCCCCCCCCCHH
59.9621906983
323UbiquitinationIIPFRALKRPLQFLG
CCCHHHCCCCHHHHH
51.49-
351UbiquitinationAYKVSGDKNEEQVLN
CEECCCCCCHHHHHH
70.55-
448PhosphorylationVVLNGMESYQEVTVQ
HHHHCCCHHCEEEEE
24.1924043423
449PhosphorylationVLNGMESYQEVTVQR
HHHCCCHHCEEEEEC
8.7224043423
526PhosphorylationGKMGFVVTMLKLIQK
HHHHHHHHHHHHHHH
16.10-
584UbiquitinationCLKEFPEKQELHRNM
HHHHCCHHHHHHHHH
49.68-
738PhosphorylationRDIIKMATARQETKE
HHHHHHHHHHHHHHH
20.9019651622
744AcetylationATARQETKEMARKVI
HHHHHHHHHHHHHHH
44.757431089
749UbiquitinationETKEMARKVIEHCSN
HHHHHHHHHHHHHHH
37.72-
758UbiquitinationIEHCSNFKEENMDTS
HHHHHHCHHHHCCCC
69.26-
764PhosphorylationFKEENMDTSR-----
CHHHHCCCCC-----
18.6829214152
765PhosphorylationKEENMDTSR------
HHHHCCCCC------
31.5629214152

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 ZER1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZER1_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 ZER1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL2_HUMANCUL2physical
17304241
CUL2_HUMANCUL2physical
18187417
ELOB_HUMANTCEB2physical
18187417
ELOC_HUMANTCEB1physical
18187417

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 ZER1_HUMAN

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Related Literatures of Post-Translational Modification

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