UBE2Z_HUMAN - dbPTM
UBE2Z_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBE2Z_HUMAN
UniProt AC Q9H832
Protein Name Ubiquitin-conjugating enzyme E2 Z
Gene Name UBE2Z
Organism Homo sapiens (Human).
Sequence Length 354
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation..
Protein Sequence MAESPTEEAATAGAGAAGPGASSVAGVVGVSGSGGGFGPPFLPDVWAAAAAAGGAGGPGSGLAPLPGLPPSAAAHGAALLSHWDPTLSSDWDGERTAPQCLLRIKRDIMSIYKEPPPGMFVVPDTVDMTKIHALITGPFDTPYEGGFFLFVFRCPPDYPIHPPRVKLMTTGNNTVRFNPNFYRNGKVCLSILGTWTGPAWSPAQSISSVLISIQSLMTENPYHNEPGFEQERHPGDSKNYNECIRHETIRVAVCDMMEGKCPCPEPLRGVMEKSFLEYYDFYEVACKDRLHLQGQTMQDPFGEKRGHFDYQSLLMRLGLIRQKVLERLHNENAEMDSDSSSSGTETDLHGSLRV
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
58 (in isoform 2)Ubiquitination-32.6221890473
110PhosphorylationRIKRDIMSIYKEPPP
HHHHHHHHHHCCCCC
24.0928348404
113 (in isoform 1)Ubiquitination-63.1721890473
113UbiquitinationRDIMSIYKEPPPGMF
HHHHHHHCCCCCCEE
63.1721906983
125PhosphorylationGMFVVPDTVDMTKIH
CEEECCCCCCCCEEE
16.6020068231
129PhosphorylationVPDTVDMTKIHALIT
CCCCCCCCEEEEEEE
23.5320068231
166 (in isoform 1)Ubiquitination-33.5421890473
166MalonylationPIHPPRVKLMTTGNN
CCCCCCEEEEECCCC
33.5426320211
166UbiquitinationPIHPPRVKLMTTGNN
CCCCCCEEEEECCCC
33.5423000965
174PhosphorylationLMTTGNNTVRFNPNF
EEECCCCEEECCCCC
19.6320068231
196 (in isoform 2)Ubiquitination-32.8821890473
238AcetylationERHPGDSKNYNECIR
CCCCCCCCCHHHHHH
69.0926051181
238UbiquitinationERHPGDSKNYNECIR
CCCCCCCCCHHHHHH
69.0921963094
240PhosphorylationHPGDSKNYNECIRHE
CCCCCCCHHHHHHHC
18.9728152594
260UbiquitinationVCDMMEGKCPCPEPL
HHHHHCCCCCCCHHC
23.0021963094
268MethylationCPCPEPLRGVMEKSF
CCCCHHCCHHHHHHH
46.50115919397
273UbiquitinationPLRGVMEKSFLEYYD
HCCHHHHHHHHHHEE
28.5421963094
287UbiquitinationDFYEVACKDRLHLQG
EHHHHHCCCCCEECC
35.8232015554
3042-HydroxyisobutyrylationMQDPFGEKRGHFDYQ
CCCCCCCCCCCCCHH
65.15-
304AcetylationMQDPFGEKRGHFDYQ
CCCCCCCCCCCCCHH
65.1523954790
304 (in isoform 1)Ubiquitination-65.1521890473
304UbiquitinationMQDPFGEKRGHFDYQ
CCCCCCCCCCCCCHH
65.1523000965
337PhosphorylationNENAEMDSDSSSSGT
HCCCCCCCCCCCCCC
37.7730278072
339PhosphorylationNAEMDSDSSSSGTET
CCCCCCCCCCCCCCC
35.7530278072
340PhosphorylationAEMDSDSSSSGTETD
CCCCCCCCCCCCCCC
33.2530278072
341PhosphorylationEMDSDSSSSGTETDL
CCCCCCCCCCCCCCC
36.4224043423
342PhosphorylationMDSDSSSSGTETDLH
CCCCCCCCCCCCCCC
52.2423911959
344PhosphorylationSDSSSSGTETDLHGS
CCCCCCCCCCCCCCC
37.3524043423
346PhosphorylationSSSSGTETDLHGSLR
CCCCCCCCCCCCCCC
43.6425072903
351PhosphorylationTETDLHGSLRV----
CCCCCCCCCCC----
11.4025850435

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 UBE2Z_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBE2Z_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 UBE2Z_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PKHF2_HUMANPLEKHF2physical
16189514
R144B_HUMANRNF144Bphysical
19690564
RN103_HUMANRNF103physical
19690564
MDM2_HUMANMDM2physical
19690564
RNF41_HUMANRNF41physical
19690564
GOLI_HUMANRNF130physical
19690564
RN150_HUMANRNF150physical
19690564
HLTF_HUMANHLTFphysical
19690564
SYVN1_HUMANSYVN1physical
19690564
RN139_HUMANRNF139physical
19690564
LNX2_HUMANLNX2physical
19549727
RNF5_HUMANRNF5physical
19549727
TRAIP_HUMANTRAIPphysical
19549727
DZIP3_HUMANDZIP3physical
19549727
RAPSN_HUMANRAPSNphysical
19549727
TRI27_HUMANTRIM27physical
19549727
RN166_HUMANRNF166physical
19549727
TRI46_HUMANTRIM46physical
19549727
UBR1_HUMANUBR1physical
21816346
UBR3_HUMANUBR3physical
21816346
UBA6_HUMANUBA6physical
20975683
XPO1_HUMANXPO1physical
22939629
WDR12_HUMANWDR12physical
22939629
TRI65_HUMANTRIM65physical
19549727
HMBX1_HUMANHMBOX1physical
25416956
KAD8_HUMANAK8physical
25416956
UBA1_HUMANUBA1physical
25768649

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 UBE2Z_HUMAN

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Related Literatures of Post-Translational Modification

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