ZN133_HUMAN - dbPTM
ZN133_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN133_HUMAN
UniProt AC P52736
Protein Name Zinc finger protein 133
Gene Name ZNF133
Organism Homo sapiens (Human).
Sequence Length 654
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation as a repressor..
Protein Sequence MAFRDVAVDFTQDEWRLLSPAQRTLYREVMLENYSNLVSLGISFSKPELITQLEQGKETWREEKKCSPATCPADPEPELYLDPFCPPGFSSQKFPMQHVLCNHPPWIFTCLCAEGNIQPGDPGPGDQEKQQQASEGRPWSDQAEGPEGEGAMPLFGRTKKRTLGAFSRPPQRQPVSSRNGLRGVELEASPAQSGNPEETDKLLKRIEVLGFGTVNCGECGLSFSKMTNLLSHQRIHSGEKPYVCGVCEKGFSLKKSLARHQKAHSGEKPIVCRECGRGFNRKSTLIIHERTHSGEKPYMCSECGRGFSQKSNLIIHQRTHSGEKPYVCRECGKGFSQKSAVVRHQRTHLEEKTIVCSDCGLGFSDRSNLISHQRTHSGEKPYACKECGRCFRQRTTLVNHQRTHSKEKPYVCGVCGHSFSQNSTLISHRRTHTGEKPYVCGVCGRGFSLKSHLNRHQNIHSGEKPIVCKDCGRGFSQQSNLIRHQRTHSGEKPMVCGECGRGFSQKSNLVAHQRTHSGERPYVCRECGRGFSHQAGLIRHKRKHSREKPYMCRQCGLGFGNKSALITHKRAHSEEKPCVCRECGQGFLQKSHLTLHQMTHTGEKPYVCKTCGRGFSLKSHLSRHRKTTSVHHRLPVQPDPEPCAGQPSDSLYSL
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
19PhosphorylationQDEWRLLSPAQRTLY
HHHHHHCCHHHHHHH
23.8423312004
34PhosphorylationREVMLENYSNLVSLG
HHHHHHCHHCHHHHC
6.91-
43PhosphorylationNLVSLGISFSKPELI
CHHHHCCCCCCHHHH
22.9724719451
201AcetylationGNPEETDKLLKRIEV
CCHHHHHHHHHHEEE
64.2410702417
222PhosphorylationNCGECGLSFSKMTNL
CCCCCCCCHHHHHHH
16.8624719451
268SumoylationQKAHSGEKPIVCREC
HHHHCCCCCEEEEEC
43.50-
268SumoylationQKAHSGEKPIVCREC
HHHHCCCCCEEEEEC
43.50-
310SumoylationCGRGFSQKSNLIIHQ
CCCCCCCCCCEEEEE
39.8628112733
324SumoylationQRTHSGEKPYVCREC
ECCCCCCCCEEECCC
45.21-
324SumoylationQRTHSGEKPYVCREC
ECCCCCCCCEEECCC
45.21-
338SumoylationCGKGFSQKSAVVRHQ
CCCCCCHHHHHHHHC
38.9028112733
367PhosphorylationGLGFSDRSNLISHQR
CCCCCCCCCCCCCCC
40.7629978859
371PhosphorylationSDRSNLISHQRTHSG
CCCCCCCCCCCCCCC
19.4129978859
375PhosphorylationNLISHQRTHSGEKPY
CCCCCCCCCCCCCCC
17.5229978859
377PhosphorylationISHQRTHSGEKPYAC
CCCCCCCCCCCCCCH
48.2929978859
424PhosphorylationHSFSQNSTLISHRRT
CCCCCCCCEEECCCC
35.34-
427PhosphorylationSQNSTLISHRRTHTG
CCCCCEEECCCCCCC
17.66-
431PhosphorylationTLISHRRTHTGEKPY
CEEECCCCCCCCCCE
24.60-
433PhosphorylationISHRRTHTGEKPYVC
EECCCCCCCCCCEEE
46.56-
461PhosphorylationNRHQNIHSGEKPIVC
HCCCCCCCCCCCEEE
44.8728555341
506SumoylationCGRGFSQKSNLVAHQ
CCCCCCHHCCCEEEE
39.86-
506SumoylationCGRGFSQKSNLVAHQ
CCCCCCHHCCCEEEE
39.8628112733
516PhosphorylationLVAHQRTHSGERPYV
CEEEECCCCCCCCEE
35.6724719451
517PhosphorylationVAHQRTHSGERPYVC
EEEECCCCCCCCEEC
41.5624719451
541MethylationQAGLIRHKRKHSREK
HHHHHHCCCCCCCCC
53.98-
576SumoylationKRAHSEEKPCVCREC
CCCCCCCCCEEECCC
39.4028112733
601PhosphorylationTLHQMTHTGEKPYVC
EEEECCCCCCCCEEE
37.56-
604SumoylationQMTHTGEKPYVCKTC
ECCCCCCCCEEECCC
42.8928112733
604SumoylationQMTHTGEKPYVCKTC
ECCCCCCCCEEECCC
42.89-
606PhosphorylationTHTGEKPYVCKTCGR
CCCCCCCEEECCCCC
29.5522817900
618SumoylationCGRGFSLKSHLSRHR
CCCCEEHHHHHHHCC
34.3328112733
618SumoylationCGRGFSLKSHLSRHR
CCCCEEHHHHHHHCC
34.33-

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 ZN133_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN133_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 ZN133_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIF1B_HUMANTRIM28physical
8769649
KR107_HUMANKRTAP10-7physical
25416956
MRS2_HUMANMRS2physical
28514442
RS27A_HUMANRPS27Aphysical
28514442
SAV1_HUMANSAV1physical
28514442
STK3_HUMANSTK3physical
28514442
TIF1A_HUMANTRIM24physical
28514442
RT07_HUMANMRPS7physical
28514442
STK4_HUMANSTK4physical
28514442
RT29_HUMANDAP3physical
28514442
CLPP_HUMANCLPPphysical
28514442
RT02_HUMANMRPS2physical
28514442
FRIL_HUMANFTLphysical
28514442
RT23_HUMANMRPS23physical
28514442
TPD52_HUMANTPD52physical
28514442

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 ZN133_HUMAN

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Related Literatures of Post-Translational Modification

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