ZN397_HUMAN - dbPTM
ZN397_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN397_HUMAN
UniProt AC Q8NF99
Protein Name Zinc finger protein 397
Gene Name ZNF397
Organism Homo sapiens (Human).
Sequence Length 534
Subcellular Localization Isoform 1: Nucleus.
Isoform 3: Nucleus. Cytoplasm.
Protein Description Isoform 3 acts as a DNA-dependent transcriptional repressor..
Protein Sequence MAVESGVISTLIPQDPPEQELILVKVEDNFSWDEKFKQNGSTQSCQELFRQQFRKFCYQETPGPREALSRLQELCYQWLMPELHTKEQILELLVLEQFLSILPEELQIWVQQHNPESGEEAVTLLEDLEREFDDPGQQVPASPQGPAVPWKDLTCLRASQESTDIHLQPLKTQLKSWKPCLSPKSDCENSETATKEGISEEKSQGLPQEPSFRGISEHESNLVWKQGSATGEKLRSPSQGGSFSQVIFTNKSLGKRDLYDEAERCLILTTDSIMCQKVPPEERPYRCDVCGHSFKQHSSLTQHQRIHTGEKPYKCNQCGKAFSLRSYLIIHQRIHSGEKAYECSECGKAFNQSSALIRHRKIHTGEKACKCNECGKAFSQSSYLIIHQRIHTGEKPYECNECGKTFSQSSKLIRHQRIHTGERPYECNECGKAFRQSSELITHQRIHSGEKPYECSECGKAFSLSSNLIRHQRIHSGEEPYQCNECGKTFKRSSALVQHQRIHSGDEAYICNECGKAFRHRSVLMRHQRVHTIK
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
31PhosphorylationVKVEDNFSWDEKFKQ
EEEECCCCCCHHHHH		39.6128112733
35UbiquitinationDNFSWDEKFKQNGST
CCCCCCHHHHHCCCH		56.2221906983
35 (in isoform 3)Ubiquitination-56.2221906983
35 (in isoform 2)Ubiquitination-56.2221906983
35 (in isoform 1)Ubiquitination-56.2221890473
37UbiquitinationFSWDEKFKQNGSTQS
CCCCHHHHHCCCHHH		54.65-
55SumoylationLFRQQFRKFCYQETP
HHHHHHHHHHCCCCC		40.8628112733
55UbiquitinationLFRQQFRKFCYQETP
HHHHHHHHHHCCCCC		40.86-
142PhosphorylationPGQQVPASPQGPAVP
CCCCCCCCCCCCCCC		16.2227499020
159PhosphorylationDLTCLRASQESTDIH
HCEEEECCCCCCCCC		28.2217525332
162PhosphorylationCLRASQESTDIHLQP
EEECCCCCCCCCCCC		24.6023312004
163PhosphorylationLRASQESTDIHLQPL
EECCCCCCCCCCCCH		37.9123312004
171SumoylationDIHLQPLKTQLKSWK
CCCCCCHHHHHHHCC		40.6928112733
176PhosphorylationPLKTQLKSWKPCLSP
CHHHHHHHCCCCCCC		49.2623312004
182PhosphorylationKSWKPCLSPKSDCEN
HHCCCCCCCCHHHCC		36.6825159151
185PhosphorylationKPCLSPKSDCENSET
CCCCCCCHHHCCCHH		51.3725159151
190PhosphorylationPKSDCENSETATKEG
CCHHHCCCHHHCCCC		17.6530576142
202SumoylationKEGISEEKSQGLPQE
CCCCCHHHHCCCCCC		43.9928112733
202UbiquitinationKEGISEEKSQGLPQE
CCCCCHHHHCCCCCC		43.9929967540
203PhosphorylationEGISEEKSQGLPQEP
CCCCHHHHCCCCCCC		32.5327251275
211PhosphorylationQGLPQEPSFRGISEH
CCCCCCCCCCCCCHH		27.1628985074
224 (in isoform 2)Phosphorylation-7.16-
225 (in isoform 1)Ubiquitination-36.9821890473
225UbiquitinationHESNLVWKQGSATGE
HHCCCEEECCCCCCC		36.9822817900
230PhosphorylationVWKQGSATGEKLRSP
EEECCCCCCCCCCCC		47.79-
236PhosphorylationATGEKLRSPSQGGSF
CCCCCCCCCCCCCCH		39.0625159151
238PhosphorylationGEKLRSPSQGGSFSQ
CCCCCCCCCCCCHHH		42.5830108239
242PhosphorylationRSPSQGGSFSQVIFT
CCCCCCCCHHHEEEE		28.6628450419
244UbiquitinationPSQGGSFSQVIFTNK
CCCCCCHHHEEEECC		25.8221890473
244PhosphorylationPSQGGSFSQVIFTNK
CCCCCCHHHEEEECC		25.8228450419
249PhosphorylationSFSQVIFTNKSLGKR
CHHHEEEECCCCCCC		30.5226074081
251SumoylationSQVIFTNKSLGKRDL
HHEEEECCCCCCCCC		43.9628112733
298PhosphorylationGHSFKQHSSLTQHQR
CCCCCCCCCCCCCCC		25.25-
308PhosphorylationTQHQRIHTGEKPYKC
CCCCCCCCCCCCEEC		44.6729496963
339UbiquitinationQRIHSGEKAYECSEC
EECCCCCCEEEHHHH		60.85-
353PhosphorylationCGKAFNQSSALIRHR
HHHHHCCCHHHHHCC		20.7730001349
354PhosphorylationGKAFNQSSALIRHRK
HHHHCCCHHHHHCCC		19.8230001349
367AcetylationRKIHTGEKACKCNEC
CCCCCCCCCEECCCC		61.507685211
381PhosphorylationCGKAFSQSSYLIIHQ
CCCCHHCCCEEEEEE		21.5428122231
382PhosphorylationGKAFSQSSYLIIHQR
CCCHHCCCEEEEEEE		19.1328122231
392PhosphorylationIIHQRIHTGEKPYEC
EEEEEEECCCCCEEC		44.6728152594
395UbiquitinationQRIHTGEKPYECNEC
EEEECCCCCEECCCC		55.00-
397PhosphorylationIHTGEKPYECNECGK
EECCCCCEECCCCCC		44.1528152594
420PhosphorylationIRHQRIHTGERPYEC
HHHCCCCCCCCCCCC		38.0628348404
432UbiquitinationYECNECGKAFRQSSE
CCCCHHHHHHHHHHH		56.88-
448PhosphorylationITHQRIHSGEKPYEC
HCCCCCCCCCCCEEC		46.4028348404
451UbiquitinationQRIHSGEKPYECSEC
CCCCCCCCCEECCCC		57.32-
456PhosphorylationGEKPYECSECGKAFS
CCCCEECCCCCCEEE		24.79-
466PhosphorylationGKAFSLSSNLIRHQR
CCEEECCCCCHHCCC		40.7327251275
476PhosphorylationIRHQRIHSGEEPYQC
HHCCCCCCCCCCCCC		45.5928985074
516UbiquitinationYICNECGKAFRHRSV
EEECCCHHHHHHHHH		56.88-
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 ZN397_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN397_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 ZN397_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STK40_HUMANSTK40physical
26186194
ZKSC3_HUMANZKSCAN3physical
26186194
ZKSC1_HUMANZKSCAN1physical
26186194
ZNF24_HUMANZNF24physical
26186194
ZKSC8_HUMANZKSCAN8physical
26186194
SCND3_HUMANZBED9physical
26186194
ZN232_HUMANZNF232physical
26186194
ZSC21_HUMANZSCAN21physical
26186194
P3H1_HUMANP3H1physical
26186194
ZN197_HUMANZNF197physical
26186194
WDR11_HUMANWDR11physical
26186194
ZN444_HUMANZNF444physical
26186194
ZN446_HUMANZNF446physical
26186194
ZN174_HUMANZNF174physical
26186194
SNX1_HUMANSNX1physical
26186194
RFWD2_HUMANRFWD2physical
26186194
ZN496_HUMANZNF496physical
26186194
ZN500_HUMANZNF500physical
26186194
F91A1_HUMANFAM91A1physical
26186194
ZSC30_HUMANZSCAN30physical
26186194
ZSC20_HUMANZSCAN20physical
26186194
SCND1_HUMANSCAND1physical
26186194
ZKSC4_HUMANZKSCAN4physical
26186194
PGBD1_HUMANPGBD1physical
26186194
ZN213_HUMANZNF213physical
26186194
ZN394_HUMANZNF394physical
26186194
ZN263_HUMANZNF263physical
26186194
ZSC29_HUMANZSCAN29physical
26186194
ZSC20_HUMANZSCAN20physical
28514442
ZN232_HUMANZNF232physical
28514442
ZN174_HUMANZNF174physical
28514442
ZN213_HUMANZNF213physical
28514442
ZSC30_HUMANZSCAN30physical
28514442
ZKSC4_HUMANZKSCAN4physical
28514442
ZN446_HUMANZNF446physical
28514442
ZKSC3_HUMANZKSCAN3physical
28514442
ZN197_HUMANZNF197physical
28514442
ZKSC1_HUMANZKSCAN1physical
28514442
ZN444_HUMANZNF444physical
28514442
SCND1_HUMANSCAND1physical
28514442
ZN496_HUMANZNF496physical
28514442
ZSC21_HUMANZSCAN21physical
28514442
ZKSC8_HUMANZKSCAN8physical
28514442
ZNF24_HUMANZNF24physical
28514442
RFWD2_HUMANRFWD2physical
28514442
ZN394_HUMANZNF394physical
28514442
PGBD1_HUMANPGBD1physical
28514442
STK40_HUMANSTK40physical
28514442
ZN500_HUMANZNF500physical
28514442
WDR11_HUMANWDR11physical
28514442
1433G_HUMANYWHAGphysical
28514442
SNX1_HUMANSNX1physical
28514442
F91A1_HUMANFAM91A1physical
28514442
1433Z_HUMANYWHAZphysical
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 ZN397_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-159, AND MASSSPECTROMETRY.

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