SZRD1_HUMAN - dbPTM
SZRD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SZRD1_HUMAN
UniProt AC Q7Z422
Protein Name SUZ domain-containing protein 1
Gene Name SZRD1
Organism Homo sapiens (Human).
Sequence Length 152
Subcellular Localization
Protein Description
Protein Sequence MEDEEVAESWEEAADSGEIDRRLEKKLKITQKESRKSKSPPKVPIVIQDDSLPAGPPPQIRILKRPTSNGVVSSPNSTSRPTLPVKSLAQREAEYAEARKRILGSASPEEEQEKPILDRPTRISQPEDSRQPNNVIRQPLGPDGSQGFKQRR
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
1Acetylation-------MEDEEVAE
-------CCHHHHHH
19413330
9PhosphorylationEDEEVAESWEEAADS
CHHHHHHHHHHHHHH
28348404
13 (in isoform 4)Phosphorylation--
17 (in isoform 2)Phosphorylation-29743597
18 (in isoform 4)Phosphorylation-29116813
19 (in isoform 2)Phosphorylation-29743597
19 (in isoform 3)Phosphorylation-22496350
20 (in isoform 4)Phosphorylation-29116813
21 (in isoform 3)Phosphorylation-22496350
34PhosphorylationLKITQKESRKSKSPP
HCCCHHHHHCCCCCC
24719451
37PhosphorylationTQKESRKSKSPPKVP
CHHHHHCCCCCCCCC
23927012
38 (in isoform 5)Phosphorylation-25849741
39PhosphorylationKESRKSKSPPKVPIV
HHHHCCCCCCCCCEE
29255136
51PhosphorylationPIVIQDDSLPAGPPP
CEEECCCCCCCCCCC
22167270
67PhosphorylationIRILKRPTSNGVVSS
EEEEECCCCCCCCCC
30266825
68PhosphorylationRILKRPTSNGVVSSP
EEEECCCCCCCCCCC
30266825
73PhosphorylationPTSNGVVSSPNSTSR
CCCCCCCCCCCCCCC
25159151
73O-linked_GlycosylationPTSNGVVSSPNSTSR
CCCCCCCCCCCCCCC
31373491
74PhosphorylationTSNGVVSSPNSTSRP
CCCCCCCCCCCCCCC
25159151
77PhosphorylationGVVSSPNSTSRPTLP
CCCCCCCCCCCCCCC
25159151
78PhosphorylationVVSSPNSTSRPTLPV
CCCCCCCCCCCCCCH
21712546
79PhosphorylationVSSPNSTSRPTLPVK
CCCCCCCCCCCCCHH
21712546
82PhosphorylationPNSTSRPTLPVKSLA
CCCCCCCCCCHHHHH
22199227
95PhosphorylationLAQREAEYAEARKRI
HHHHHHHHHHHHHHH
28796482
104PhosphorylationEARKRILGSASPEEE
HHHHHHHCCCCCHHH
32142685
105PhosphorylationARKRILGSASPEEEQ
HHHHHHCCCCCHHHH
29255136
106PhosphorylationRKRILGSASPEEEQE
HHHHHCCCCCHHHHC
33259812
107O-linked_GlycosylationKRILGSASPEEEQEK
HHHHCCCCCHHHHCC
OGP
107PhosphorylationKRILGSASPEEEQEK
HHHHCCCCCHHHHCC
29255136
113UbiquitinationASPEEEQEKPILDRP
CCCHHHHCCCCCCCC
29967540
114UbiquitinationSPEEEQEKPILDRPT
CCHHHHCCCCCCCCC
29967540
121PhosphorylationKPILDRPTRISQPED
CCCCCCCCCCCCCCC
25159151
121O-linked_GlycosylationKPILDRPTRISQPED
CCCCCCCCCCCCCCC
OGP
124PhosphorylationLDRPTRISQPEDSRQ
CCCCCCCCCCCCCCC
21815630
129PhosphorylationRISQPEDSRQPNNVI
CCCCCCCCCCCCCCC
21712546
148UbiquitinationGPDGSQGFKQRR---
CCCCCCCCCCCC---
24816145
149UbiquitinationPDGSQGFKQRR----
CCCCCCCCCCC----
24816145
149MethylationPDGSQGFKQRR----
CCCCCCCCCCC----
115980257

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 SZRD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SZRD1_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 SZRD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTMR2_HUMANMTMR2physical
22863883
5NTC_HUMANNT5C2physical
22863883
SRP14_HUMANSRP14physical
22863883
SRP09_HUMANSRP9physical
22863883
ZPR1_HUMANZPR1physical
22863883

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 SZRD1_HUMAN

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Related Literatures of Post-Translational Modification

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