ZN574_HUMAN - dbPTM
ZN574_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN574_HUMAN
UniProt AC Q6ZN55
Protein Name Zinc finger protein 574
Gene Name ZNF574
Organism Homo sapiens (Human).
Sequence Length 896
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MTEESEETVLYIEHRYVCSECNQLYGSLEEVLMHQNSHVPQQHFELVGVADPGVTVATDTASGTGLYQTLVQESQYQCLECGQLLMSPSQLLEHQELHLKMMAPQEAVPAEPSPKAPPLSSSTIHYECVDCKALFASQELWLNHRQTHLRATPTKAPAPVVLGSPVVLGPPVGQARVAVEHSYRKAEEGGEGATVPSAAATTTEVVTEVELLLYKCSECSQLFQLPADFLEHQATHFPAPVPESQEPALQQEVQASSPAEVPVSQPDPLPASDHSYELRNGEAIGRDRRGRRARRNNSGEAGGAATQELFCSACDQLFLSPHQLQQHLRSHREGVFKCPLCSRVFPSPSSLDQHLGDHSSESHFLCVDCGLAFGTEALLLAHRRAHTPNPLHSCPCGKTFVNLTKFLYHRRTHGVGGVPLPTTPVPPEEPVIGFPEPAPAETGEPEAPEPPVSEETSAGPAAPGTYRCLLCSREFGKALQLTRHQRFVHRLERRHKCSICGKMFKKKSHVRNHLRTHTGERPFPCPDCSKPFNSPANLARHRLTHTGERPYRCGDCGKAFTQSSTLRQHRLVHAQHFPYRCQECGVRFHRPYRLLMHRYHHTGEYPYKCRECPRSFLLRRLLEVHQLVVHAGRQPHRCPSCGAAFPSSLRLREHRCAAAAAQAPRRFECGTCGKKVGSAARLQAHEAAHAAAGPGEVLAKEPPAPRAPRATRAPVASPAALGSTATASPAAPARRRGLECSECKKLFSTETSLQVHRRIHTGERPYPCPDCGKAFRQSTHLKDHRRLHTGERPFACEVCGKAFAISMRLAEHRRIHTGERPYSCPDCGKSYRSFSNLWKHRKTHQQQHQAAVRQQLAEAEAAVGLAVMETAVEALPLVEAIEIYPLAEAEGVQISG
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
2Phosphorylation------MTEESEETV
------CCCCHHHHE		48.7530108239
5Phosphorylation---MTEESEETVLYI
---CCCCHHHHEEEE		34.2030108239
113PhosphorylationEAVPAEPSPKAPPLS
CCCCCCCCCCCCCCC		30.4525159151
137PhosphorylationDCKALFASQELWLNH
CHHHHHHCHHHHHHC		19.4917525332
147PhosphorylationLWLNHRQTHLRATPT
HHHHCCCHHCCCCCC		23.8828464451
152PhosphorylationRQTHLRATPTKAPAP
CCHHCCCCCCCCCCC		25.6723927012
154PhosphorylationTHLRATPTKAPAPVV
HHCCCCCCCCCCCEE		35.1723927012
164PhosphorylationPAPVVLGSPVVLGPP
CCCEECCCCEEECCC		15.4528355574
183PhosphorylationRVAVEHSYRKAEEGG
HHHHHHHHHHHHHCC		20.31-
256PhosphorylationLQQEVQASSPAEVPV
HHHHHHHCCCCCCCC		21.5526074081
257PhosphorylationQQEVQASSPAEVPVS
HHHHHHCCCCCCCCC		31.0126074081
264PhosphorylationSPAEVPVSQPDPLPA
CCCCCCCCCCCCCCC		29.9026074081
298PhosphorylationRRARRNNSGEAGGAA
CCCCCCCCCCCCCHH		41.3722617229
306PhosphorylationGEAGGAATQELFCSA
CCCCCHHHHHHHHHH		23.2622617229
312PhosphorylationATQELFCSACDQLFL
HHHHHHHHHHHHHCC		25.2928464451
320PhosphorylationACDQLFLSPHQLQQH
HHHHHCCCHHHHHHH		17.0120068231
387 (in isoform 2)Phosphorylation-24.6321406692
387PhosphorylationLAHRRAHTPNPLHSC
HHHHHCCCCCCCCCC		24.6328985074
405 (in isoform 1)Ubiquitination-36.2221890473
405UbiquitinationKTFVNLTKFLYHRRT
HHHHHHHHHHHCCCC		36.222189047
409 (in isoform 2)Phosphorylation-18.2021406692
422PhosphorylationVGGVPLPTTPVPPEE
CCCCCCCCCCCCCCC		51.9528348404
423PhosphorylationGGVPLPTTPVPPEEP
CCCCCCCCCCCCCCC		21.9828348404
477SumoylationLCSREFGKALQLTRH
EEEHHHHHHHHHHHH		51.77-
477UbiquitinationLCSREFGKALQLTRH
EEEHHHHHHHHHHHH		51.77-
477SumoylationLCSREFGKALQLTRH
EEEHHHHHHHHHHHH		51.77-
494 (in isoform 2)Ubiquitination-25.0021890473
495 (in isoform 2)Ubiquitination-41.5221890473
502AcetylationHKCSICGKMFKKKSH
HCCCCCHHHHCCHHH		36.4330593797
506AcetylationICGKMFKKKSHVRNH
CCHHHHCCHHHHHHH		48.5230593803
507AcetylationCGKMFKKKSHVRNHL
CHHHHCCHHHHHHHH		46.5130593809
508PhosphorylationGKMFKKKSHVRNHLR
HHHHCCHHHHHHHHH		35.77-
518PhosphorylationRNHLRTHTGERPFPC
HHHHHHCCCCCCCCC		39.8725159151
530UbiquitinationFPCPDCSKPFNSPAN
CCCCCCCCCCCCHHH		61.02-
534PhosphorylationDCSKPFNSPANLARH
CCCCCCCCHHHHHHH		26.2622199227
544PhosphorylationNLARHRLTHTGERPY
HHHHHCCCCCCCCCE		19.8328348404
546PhosphorylationARHRLTHTGERPYRC
HHHCCCCCCCCCEEC		35.1929214152
558UbiquitinationYRCGDCGKAFTQSST
EECCCCCCCCCCCHH		46.81-
566 (in isoform 2)Ubiquitination-5.54-
602PhosphorylationLMHRYHHTGEYPYKC
HEECCCCCCCCCCCC		20.5629214152
605PhosphorylationRYHHTGEYPYKCREC
CCCCCCCCCCCCCCC		17.1317360941
608UbiquitinationHTGEYPYKCRECPRS
CCCCCCCCCCCCCHH		23.47-
615PhosphorylationKCRECPRSFLLRRLL
CCCCCCHHHHHHHHH		12.8524719451
619 (in isoform 2)Ubiquitination-29.37-
647 (in isoform 2)Ubiquitination-35.23-
648PhosphorylationCGAAFPSSLRLREHR
CCCCCCCCHHHHHHH		20.1117081983
674AcetylationFECGTCGKKVGSAAR
EECCCCCCCCCHHHH		46.5730593791
697 (in isoform 2)Ubiquitination-8.58-
700UbiquitinationGPGEVLAKEPPAPRA
CCCCHHCCCCCCCCC		67.60-
711PhosphorylationAPRAPRATRAPVASP
CCCCCCCCCCCCCCH		28.7423090842
717PhosphorylationATRAPVASPAALGST
CCCCCCCCHHHHCCC		18.4625159151
723PhosphorylationASPAALGSTATASPA
CCHHHHCCCCCCCCC		18.7325159151
724PhosphorylationSPAALGSTATASPAA
CHHHHCCCCCCCCCC		26.6516964243
726PhosphorylationAALGSTATASPAAPA
HHHCCCCCCCCCCHH		27.9622199227
728PhosphorylationLGSTATASPAAPARR
HCCCCCCCCCCHHHH		15.6625159151
748PhosphorylationSECKKLFSTETSLQV
HHHHHHHCCCCCHHH		35.4524247654
761PhosphorylationQVHRRIHTGERPYPC
HHHHHCCCCCCCCCC		38.0628985074
779PhosphorylationGKAFRQSTHLKDHRR
HHHHHHCCCCCCCCC		23.9227251275
789 (in isoform 2)Ubiquitination-45.38-
789PhosphorylationKDHRRLHTGERPFAC
CCCCCCCCCCCCCHH		45.3825159151
806PhosphorylationCGKAFAISMRLAEHR
CCHHHHHHHHHHHHC		8.4024719451
817PhosphorylationAEHRRIHTGERPYSC
HHHCCCCCCCCCCCC		38.0628674419
832Asymmetric dimethylargininePDCGKSYRSFSNLWK
CCCCCCHHHHHHHHH		38.01-
832MethylationPDCGKSYRSFSNLWK
CCCCCCHHHHHHHHH		38.0124129315
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 ZN574_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN574_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 ZN574_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SHCBP_HUMANSHCBP1physical
28514442
P52K_HUMANPRKRIRphysical
28514442
TRI41_HUMANTRIM41physical
28514442
ANR28_HUMANANKRD28physical
28514442
IFFO1_HUMANIFFO1physical
28514442
PP6R2_HUMANPPP6R2physical
28514442
KBTB7_HUMANKBTBD7physical
28514442
LTBP4_HUMANLTBP4physical
28514442
KBTB6_HUMANKBTBD6physical
28514442
SART3_HUMANSART3physical
28514442
UBE2O_HUMANUBE2Ophysical
28514442
RT09_HUMANMRPS9physical
28514442
CENPB_HUMANCENPBphysical
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 ZN574_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-154; SER-164;SER-298; SER-717 AND SER-728, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; THR-724 ANDSER-728, AND MASS SPECTROMETRY.

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