ZN550_HUMAN - dbPTM
ZN550_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN550_HUMAN
UniProt AC Q7Z398
Protein Name Zinc finger protein 550
Gene Name ZNF550
Organism Homo sapiens (Human).
Sequence Length 422
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAETKDAAQMLVTFKDVAVTFTREEWRQLDLAQRTLYREVMLETCGLLVSLGHRVPKPELVHLLEHGQELWIVKRGLSHATCAGDRAQVHTREPTTYPPVLSERAFLRGSLTLESSTSSDSRLGRARDEEGLLEMQKGKVTPETDLHKETHLGKVSLEGEGLGTDDGLHSRALQEWLSADVLHECDSQQPGKDALIHAGTNPYKCKQCGKGFNRKWYLVRHQRVHTGMKPYECNACGKAFSQSSTLIRHYLIHTGEKPYKCLECGKAFKRRSYLMQHHPIHTGEKPYECSQCRKAFTHRSTFIRHNRTHTGEKPFECKECEKAFSNRAHLIQHYIIHTGEKPYDCMACGKAFRCSSELIQHQRIHTGEKPYECTQCGKAFHRSTYLIQHSVIHTGEMPYKCIECGKAFKRRSHLLQHQRVHT
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
4Phosphorylation----MAETKDAAQML
----CCCCHHHHHHH
25.3729759185
13PhosphorylationDAAQMLVTFKDVAVT
HHHHHHHHHHHHEEE
22.4729759185
20PhosphorylationTFKDVAVTFTREEWR
HHHHHEEEECHHHHH
15.0029759185
22PhosphorylationKDVAVTFTREEWRQL
HHHEEEECHHHHHHH
28.0129759185
37 (in isoform 2)Phosphorylation-12.2422210691
63 (in isoform 2)Phosphorylation-4.7122210691
78PhosphorylationWIVKRGLSHATCAGD
EEEECCCCCCCCCCC
17.5628555341
95PhosphorylationQVHTREPTTYPPVLS
EEECCCCCCCCCCCC
33.92-
96PhosphorylationVHTREPTTYPPVLSE
EECCCCCCCCCCCCC
44.75-
97PhosphorylationHTREPTTYPPVLSER
ECCCCCCCCCCCCCC
14.17-
102PhosphorylationTTYPPVLSERAFLRG
CCCCCCCCCCHHHCC
25.85-
137UbiquitinationEGLLEMQKGKVTPET
HHHHHHHCCCCCCCC
60.43-
141PhosphorylationEMQKGKVTPETDLHK
HHHCCCCCCCCCCCC
20.9229214152
148UbiquitinationTPETDLHKETHLGKV
CCCCCCCCCCCCEEE
72.1629967540
154UbiquitinationHKETHLGKVSLEGEG
CCCCCCEEEEECCCC
34.7029967540
156PhosphorylationETHLGKVSLEGEGLG
CCCCEEEEECCCCCC
24.9628555341
192UbiquitinationCDSQQPGKDALIHAG
CCCCCCCCCCEEECC
46.6529967540
215UbiquitinationCGKGFNRKWYLVRHQ
CCCCCCCEEEEEEEE
41.09-
241PhosphorylationNACGKAFSQSSTLIR
CCCCCCCCCCHHHHH
33.7322210691
243PhosphorylationCGKAFSQSSTLIRHY
CCCCCCCCHHHHHHH
24.8822210691
244PhosphorylationGKAFSQSSTLIRHYL
CCCCCCCHHHHHHHH
21.4222210691
248UbiquitinationSQSSTLIRHYLIHTG
CCCHHHHHHHHHCCC
18.6022505724
250PhosphorylationSSTLIRHYLIHTGEK
CHHHHHHHHHCCCCC
9.4822210691
254PhosphorylationIRHYLIHTGEKPYKC
HHHHHHCCCCCCEEE
39.7929496963
257UbiquitinationYLIHTGEKPYKCLEC
HHHCCCCCCEEEHHH
55.8022505724
259PhosphorylationIHTGEKPYKCLECGK
HCCCCCCEEEHHHCH
25.9615592455
260SumoylationHTGEKPYKCLECGKA
CCCCCCEEEHHHCHH
40.65-
260SumoylationHTGEKPYKCLECGKA
CCCCCCEEEHHHCHH
40.65-
266UbiquitinationYKCLECGKAFKRRSY
EEEHHHCHHHHHHHH
63.41-
272PhosphorylationGKAFKRRSYLMQHHP
CHHHHHHHHHHHCCC
27.01-
273PhosphorylationKAFKRRSYLMQHHPI
HHHHHHHHHHHCCCC
12.37-
282PhosphorylationMQHHPIHTGEKPYEC
HHCCCCCCCCCCCCC
47.99-
287PhosphorylationIHTGEKPYECSQCRK
CCCCCCCCCCHHHHH
40.4126699800
290PhosphorylationGEKPYECSQCRKAFT
CCCCCCCHHHHHHHH
22.0026699800
297PhosphorylationSQCRKAFTHRSTFIR
HHHHHHHHCCCHHCC
22.6526699800
308PhosphorylationTFIRHNRTHTGEKPF
HHCCCCCCCCCCCCC
29.16-
310PhosphorylationIRHNRTHTGEKPFEC
CCCCCCCCCCCCCCC
46.5621857030
313UbiquitinationNRTHTGEKPFECKEC
CCCCCCCCCCCCHHH
57.25-
338PhosphorylationIQHYIIHTGEKPYDC
HHHHHEECCCCCCCC
36.3127251275
356PhosphorylationGKAFRCSSELIQHQR
CCCEECCHHHHHCCC
39.7928348404
366PhosphorylationIQHQRIHTGEKPYEC
HHCCCCCCCCCCCEE
44.6728111955
394PhosphorylationIQHSVIHTGEMPYKC
EECCEEECCCCCCEE
24.58-

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 ZN550_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN550_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 ZN550_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MEIOC_HUMANC17orf104physical
28514442
ZN714_HUMANZNF714physical
28514442
YTDC2_HUMANYTHDC2physical
28514442
TRI37_HUMANTRIM37physical
28514442
ZN460_HUMANZNF460physical
28514442
ZNF92_HUMANZNF92physical
28514442
RBAK_HUMANRBAKphysical
28514442
UBP34_HUMANUSP34physical
28514442
TRI41_HUMANTRIM41physical
28514442
FBLN5_HUMANFBLN5physical
28514442
PP2AA_HUMANPPP2CAphysical
28514442
STRN4_HUMANSTRN4physical
28514442
2AAB_HUMANPPP2R1Bphysical
28514442
STRN3_HUMANSTRN3physical
28514442
SMRCD_HUMANSMARCAD1physical
28514442
CENPB_HUMANCENPBphysical
28514442
CT2NL_HUMANCTTNBP2NLphysical
28514442
SLMAP_HUMANSLMAPphysical
28514442
MDM2_HUMANMDM2physical
28514442
STRP1_HUMANSTRIP1physical
28514442
STRN_HUMANSTRNphysical
28514442
SIR1_HUMANSIRT1physical
28514442
2ABD_HUMANPPP2R2Dphysical
28514442
TIF1A_HUMANTRIM24physical
28514442
PASK_HUMANPASKphysical
28514442
ERBIN_HUMANERBB2IPphysical
28514442
LRRC1_HUMANLRRC1physical
28514442
CR025_HUMANC18orf25physical
28514442
LTBP4_HUMANLTBP4physical
28514442
2AAA_HUMANPPP2R1Aphysical
28514442
RT09_HUMANMRPS9physical
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 ZN550_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-259, AND MASSSPECTROMETRY.

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