ZN408_HUMAN - dbPTM
ZN408_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN408_HUMAN
UniProt AC Q9H9D4
Protein Name Zinc finger protein 408
Gene Name ZNF408
Organism Homo sapiens (Human).
Sequence Length 720
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MEEAEELLLEGKKALQLAREPRLGLDLGWNPSGEGCTQGLKDVPPEPTRDILALKSLPRGLALGPSLAKEQRLGVWCVGDPLQPGLLWGPLEEESASKEKGEGVKPRQEENLSLGPWGDVCACEQSSGWTSLVQRGRLESEGNVAPVRISERLHLQVYQLVLPGSELLLWPQPSSEGPSLTQPGLDKEAAVAVVTEVESAVQQEVASPGEDAAEPCIDPGSQSPSGIQAENMVSPGLKFPTQDRISKDSQPLGPLLQDGDVDEECPAQAQMPPELQSNSATQQDPDGSGASFSSSARGTQPHGYLAKKLHSPSDQCPPRAKTPEPGAQQSGFPTLSRSPPGPAGSSPKQGRRYRCGECGKAFLQLCHLKKHAFVHTGHKPFLCTECGKSYSSEESFKAHMLGHRGVRPFPCPQCDKAYGTQRDLKEHQVVHSGARPFACDQCGKAFARRPSLRLHRKTHQVPAAPAPCPCPVCGRPLANQGSLRNHMRLHTGEKPFLCPHCGRAFRQRGNLRGHLRLHTGERPYRCPHCADAFPQLPELRRHLISHTGEAHLCPVCGKALRDPHTLRAHERLHSGERPFPCPQCGRAYTLATKLRRHLKSHLEDKPYRCPTCGMGYTLPQSLRRHQLSHRPEAPCSPPSVPSAASEPTVVLLQAEPQLLDTHREEEVSPARDVVEVTISESQEKCFVVPEEPDAAPSLVLIHKDMGLGAWAEVVEVEMGT
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
225PhosphorylationDPGSQSPSGIQAENM
CCCCCCCCCCCCCCC
54.5024275569
234PhosphorylationIQAENMVSPGLKFPT
CCCCCCCCCCCCCCC
11.5024719451
311PhosphorylationYLAKKLHSPSDQCPP
CHHHHCCCCCCCCCC
36.2125159151
313PhosphorylationAKKLHSPSDQCPPRA
HHHCCCCCCCCCCCC
43.2427732954
322PhosphorylationQCPPRAKTPEPGAQQ
CCCCCCCCCCCCCHH
31.7230266825
330PhosphorylationPEPGAQQSGFPTLSR
CCCCCHHCCCCCCCC
30.2623403867
334PhosphorylationAQQSGFPTLSRSPPG
CHHCCCCCCCCCCCC
34.7923403867
336PhosphorylationQSGFPTLSRSPPGPA
HCCCCCCCCCCCCCC
32.9423403867
338PhosphorylationGFPTLSRSPPGPAGS
CCCCCCCCCCCCCCC
31.8830266825
345PhosphorylationSPPGPAGSSPKQGRR
CCCCCCCCCCCCCCC
45.6425056879
346PhosphorylationPPGPAGSSPKQGRRY
CCCCCCCCCCCCCCE
34.8928985074
432PhosphorylationKEHQVVHSGARPFAC
HHCCEECCCCCCCCC
23.6525159151
451PhosphorylationKAFARRPSLRLHRKT
HHHHHCCCCCCCCCC
25.0628258704
491PhosphorylationRNHMRLHTGEKPFLC
CCCEECCCCCCCCCC
52.1821857030
494SumoylationMRLHTGEKPFLCPHC
EECCCCCCCCCCCCC
42.27-
494SumoylationMRLHTGEKPFLCPHC
EECCCCCCCCCCCCC
42.27-
512MethylationFRQRGNLRGHLRLHT
HHHHCCCCCCEEEEC
34.1954561957
512DimethylationFRQRGNLRGHLRLHT
HHHHCCCCCCEEEEC
34.19-
519PhosphorylationRGHLRLHTGERPYRC
CCCEEEECCCCCCCC
45.38-
547PhosphorylationRRHLISHTGEAHLCP
HHHHHHHCCCCCCCC
29.9028555341
574PhosphorylationRAHERLHSGERPFPC
HHHHHHCCCCCCCCC
47.1129214152
593SumoylationRAYTLATKLRRHLKS
HHHHHHHHHHHHHHH
34.10-
593SumoylationRAYTLATKLRRHLKS
HHHHHHHHHHHHHHH
34.10-
605SumoylationLKSHLEDKPYRCPTC
HHHHHCCCCCCCCCC
34.28-
605SumoylationLKSHLEDKPYRCPTC
HHHHHCCCCCCCCCC
34.28-
628PhosphorylationSLRRHQLSHRPEAPC
HHHHHCCCCCCCCCC
15.7528348404
636PhosphorylationHRPEAPCSPPSVPSA
CCCCCCCCCCCCCCC
38.4928348404
639PhosphorylationEAPCSPPSVPSAASE
CCCCCCCCCCCCCCC
50.4728348404
668PhosphorylationTHREEEVSPARDVVE
CCCCCCCCCCCCEEE
19.0021815630
681PhosphorylationVEVTISESQEKCFVV
EEEEECCCCCCEEEC
36.5325003641

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 ZN408_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN408_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 ZN408_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RALYL_HUMANRALYLphysical
16189514
CEP70_HUMANCEP70physical
16189514
KR412_HUMANKRTAP4-12physical
16189514
ZBT8A_HUMANZBTB8Aphysical
16189514
ZBTB9_HUMANZBTB9physical
20211142
FHL2_HUMANFHL2physical
18255255
S30BP_HUMANSAP30BPphysical
18255255
ID3_HUMANID3physical
18255255
ZN408_HUMANZNF408physical
18255255
CEP70_HUMANCEP70physical
19060904
LDOC1_HUMANLDOC1physical
19060904
MDFI_HUMANMDFIphysical
19060904
GIPC1_HUMANGIPC1physical
15231747
PDLI4_HUMANPDLIM4physical
15231747
DDX56_HUMANDDX56physical
15231747
LSM2_HUMANLSM2physical
15231747
ZN408_HUMANZNF408physical
15231747
ZN330_HUMANZNF330physical
15231747
CC136_HUMANCCDC136physical
15231747
MIF_HUMANMIFphysical
15231747
TOP3B_HUMANTOP3Bphysical
15231747
CAF1A_HUMANCHAF1Aphysical
15231747
CREL1_HUMANCRELD1physical
15231747
ATRN_HUMANATRNphysical
15231747
FBLN2_HUMANFBLN2physical
15231747
PRAME_HUMANPRAMEphysical
15231747
EXOS2_HUMANEXOSC2physical
15231747
RENT2_HUMANUPF2physical
15231747
ZN408_HUMANZNF408physical
25416956
CEP70_HUMANCEP70physical
25416956
ZN792_HUMANZNF792physical
25416956
NINL_HUMANNINLphysical
28514442
FBN1_HUMANFBN1physical
28514442
SHCBP_HUMANSHCBP1physical
28514442
SMYD2_HUMANSMYD2physical
28514442
MIPO1_HUMANMIPOL1physical
28514442
SPS2_HUMANSEPHS2physical
28514442
LRP1B_HUMANLRP1Bphysical
28514442
LTBP1_HUMANLTBP1physical
28514442
LZTS2_HUMANLZTS2physical
28514442
PGBM_HUMANHSPG2physical
28514442
LRP4_HUMANLRP4physical
28514442
LTBP4_HUMANLTBP4physical
28514442
FBLN5_HUMANFBLN5physical
28514442
RS27A_HUMANRPS27Aphysical
28514442
PKCB1_HUMANZMYND8physical
28514442
APC_HUMANAPCphysical
28514442
AMER1_HUMANAMER1physical
28514442
ZBTB9_HUMANZBTB9physical
28514442
TRI41_HUMANTRIM41physical
28514442
TBA3C_HUMANTUBA3Cphysical
28514442
ZN687_HUMANZNF687physical
28514442
SORL_HUMANSORL1physical
28514442
FBXW8_HUMANFBXW8physical
28514442
VLDLR_HUMANVLDLRphysical
28514442
NELL2_HUMANNELL2physical
28514442
CUL7_HUMANCUL7physical
28514442
LDLR_HUMANLDLRphysical
28514442
MTMR4_HUMANMTMR4physical
28514442
CDC27_HUMANCDC27physical
28514442
ANC2_HUMANANAPC2physical
28514442
LRP2_HUMANLRP2physical
28514442
CXXC1_HUMANCXXC1physical
28514442
FBN2_HUMANFBN2physical
28514442
AGGF1_HUMANAGGF1physical
28514442
WDCP_HUMANC2orf44physical
28514442
NOTC3_HUMANNOTCH3physical
28514442
CDC16_HUMANCDC16physical
28514442
ZN592_HUMANZNF592physical
28514442
CDC23_HUMANCDC23physical
28514442
FRAS1_HUMANFRAS1physical
28514442
ZN460_HUMANZNF460physical
28514442
GRN_HUMANGRNphysical
28514442
ERBIN_HUMANERBB2IPphysical
28514442
CHAP1_HUMANCHAMP1physical
28514442
K0232_HUMANKIAA0232physical
28514442
CENPB_HUMANCENPBphysical
28514442
USP9X_HUMANUSP9Xphysical
28514442
LAMA1_HUMANLAMA1physical
28514442
APBP2_HUMANAPPBP2physical
28514442
RT07_HUMANMRPS7physical
28514442
RT29_HUMANDAP3physical
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 ZN408_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP