ZN609_MOUSE - dbPTM
ZN609_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN609_MOUSE
UniProt AC Q8BZ47
Protein Name Zinc finger protein 609
Gene Name Znf609
Organism Mus musculus (Mouse).
Sequence Length 1413
Subcellular Localization Nucleus .
Protein Description Transcription factor, which activates RAG1, and possibly RAG2, transcription. Through the regulation of RAG1/2 expression, may regulate thymocyte maturation. [PubMed: 28344082 Along with NIPBL and the multiprotein complex Integrator, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others]
Protein Sequence MSLSSGACGGKGVDANPVETYDSGDEWDIGVGNLIIDLDADLEKDQQKLEMSGSKEVGIPAPNAVATLPDNIKFVTPVPGPQGKEGKSKSKRSKSGKDASKPTPGTSLFSPSEGAASKKEVQGRAGDGASAGGLVAAVAPKGSEKAAKASRSVAGSKKEKENSSSKGKKERSEGVGTCSEKDPGVLQPVPLGGRGSQYDGSAGMDTGTVEPLGSIAIEPGAALNPLGTKPEPEEGENECRPLKKVKSEKMESPVSTPAVLPLHLLVPVVNNDISSPCEQIMVRTRSVGVNTCDVALATEPECLGPCEPGTSVNLEGIVWQETEDGMLVVNVTWRNKTYVGTLLDCTRHDWAPPRFCDSPTSDLEMRNGRGRGKRMRPSSNTPVSEAAAASDSKGTSSSSKTRAGANSKGRRGSQNSSEHRPPASSTSEDVKASPSSANKRKSKPLSDMELNSSSEDSKGSKRVRTNSMGSATGPLPGTKVEPTLVDRNCPSPVLIDCPHPNCNKKYKHINGLKYHQAHAHTDDDSKPEADGDSEYGEEPALHADLSCNGAPVPQKGSLSPARSATPKVRLVEPHSPSPSSKFSTKGLCKKKLSGEGDTDPGALSNDGSDDGPSVMDETSNDAFDSLERKCMEKEKCKKPSSLKSEKIPSKSLKSARPIAPAIPPQQIYTFQTATFTAASPGSSSGLTTTVVQAMPNSPQLKPIQPKPTVMGEPFTVNPALTPAKDKKKKDKKKKDSSKELESPLTPGKVCRAEEGKSPFRDAAGDGIKVESLLNGSSESHQSRLASIKAEADKIYSFTDNAPSPSIGGSSRLDSTTPTQPLTPLHVVTQNGAEASSVKTNSPAYSDISDAGEDGEGKVDSAKSKDPEQLVKEGAKKTLFPPQPQSKDSPYYQGFESYYSPGYAQSSPGTLTSSSQAGMEGQPLKTKKDEEPESVEGKVKNDVCEEKKPELSNSSQQPSVIQQRPNMYMQSLYYNQYAYVPPYGYSDQSYHSHLLSTNTAYRQQYEEQQKRQSLEQQQQQQRGLDKKTEMGLKEREASLKEEWKQKPSIPPTLTKAPSLTDLVKSGPGKAKEPGTDPAKSVIIPKLDDSSKLPSQPPEGLKGKLGEASHLGKEASEAKTGTECGRQAEVDPILWYRQETESRMWTYVYPAKYSDIKSEDDRWKEERDRKLKEDRSRSKDSVPKEDGKESTSSDCKLPPSEESRLGSKEPRPSVHVPVSSPLTQHQSYIPYMHGYSYSQSYDPNHPSYRGMPAVMMQNYPGSYLPSSYSFSPYGSKVSGGEDADKARASPSVSCKASSESKALDILQQHASHYKSKSPTISDKNSQERDRGGCGVVGGGGSCGSVAGAGGTDRSADRPRTSPSQRLMSTHHHHHHLGYSLLPAQYNLPYAAGLSSTAIVASQQGSTPSLYPPPRR
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
100PhosphorylationSKSGKDASKPTPGTS
CCCCCCCCCCCCCCC
49.6728066266
103PhosphorylationGKDASKPTPGTSLFS
CCCCCCCCCCCCCCC
37.7828066266
106PhosphorylationASKPTPGTSLFSPSE
CCCCCCCCCCCCCCC
24.3828066266
107PhosphorylationSKPTPGTSLFSPSEG
CCCCCCCCCCCCCCC
33.0728066266
110PhosphorylationTPGTSLFSPSEGAAS
CCCCCCCCCCCCCCC
32.5828066266
112PhosphorylationGTSLFSPSEGAASKK
CCCCCCCCCCCCCCC
47.6828066266
117PhosphorylationSPSEGAASKKEVQGR
CCCCCCCCCCCCCCC
43.6728066266
130PhosphorylationGRAGDGASAGGLVAA
CCCCCCCCCCCCEEE
32.7325159016
252PhosphorylationVKSEKMESPVSTPAV
HCCCCCCCCCCCCCE
27.4026239621
255PhosphorylationEKMESPVSTPAVLPL
CCCCCCCCCCCEEEH
31.8623649490
256PhosphorylationKMESPVSTPAVLPLH
CCCCCCCCCCEEEHH
18.5926643407
358PhosphorylationAPPRFCDSPTSDLEM
CCCCCCCCCCCCCCC
31.1225521595
360PhosphorylationPRFCDSPTSDLEMRN
CCCCCCCCCCCCCCC
38.5321082442
361PhosphorylationRFCDSPTSDLEMRNG
CCCCCCCCCCCCCCC
43.5121082442
378PhosphorylationRGKRMRPSSNTPVSE
CCCCCCCCCCCCHHH
26.3426643407
379PhosphorylationGKRMRPSSNTPVSEA
CCCCCCCCCCCHHHH
47.6226643407
381PhosphorylationRMRPSSNTPVSEAAA
CCCCCCCCCHHHHHH
27.3226643407
390PhosphorylationVSEAAAASDSKGTSS
HHHHHHHCCCCCCCC
37.3829514104
413PhosphorylationNSKGRRGSQNSSEHR
CCCCCCCCCCCCCCC
25.1126824392
416PhosphorylationGRRGSQNSSEHRPPA
CCCCCCCCCCCCCCC
29.4829472430
417PhosphorylationRRGSQNSSEHRPPAS
CCCCCCCCCCCCCCC
45.0029472430
424PhosphorylationSEHRPPASSTSEDVK
CCCCCCCCCCCCHHC
39.6625777480
425PhosphorylationEHRPPASSTSEDVKA
CCCCCCCCCCCHHCC
37.7525777480
426PhosphorylationHRPPASSTSEDVKAS
CCCCCCCCCCHHCCC
33.3725777480
427PhosphorylationRPPASSTSEDVKASP
CCCCCCCCCHHCCCC
33.4729472430
433PhosphorylationTSEDVKASPSSANKR
CCCHHCCCCCCCCCC
21.43-
435PhosphorylationEDVKASPSSANKRKS
CHHCCCCCCCCCCCC
39.32-
436PhosphorylationDVKASPSSANKRKSK
HHCCCCCCCCCCCCC
38.96-
442PhosphorylationSSANKRKSKPLSDME
CCCCCCCCCCCCCCC
43.4725619855
446PhosphorylationKRKSKPLSDMELNSS
CCCCCCCCCCCCCCC
43.3625619855
452PhosphorylationLSDMELNSSSEDSKG
CCCCCCCCCCCCCCC
48.1125619855
453PhosphorylationSDMELNSSSEDSKGS
CCCCCCCCCCCCCCC
36.3525619855
454PhosphorylationDMELNSSSEDSKGSK
CCCCCCCCCCCCCCC
45.2925619855
457PhosphorylationLNSSSEDSKGSKRVR
CCCCCCCCCCCCCCC
34.5625619855
460PhosphorylationSSEDSKGSKRVRTNS
CCCCCCCCCCCCCCC
22.4825619855
465PhosphorylationKGSKRVRTNSMGSAT
CCCCCCCCCCCCCCC
28.8723527152
467PhosphorylationSKRVRTNSMGSATGP
CCCCCCCCCCCCCCC
24.7325521595
470PhosphorylationVRTNSMGSATGPLPG
CCCCCCCCCCCCCCC
17.6428833060
472PhosphorylationTNSMGSATGPLPGTK
CCCCCCCCCCCCCCC
40.8228833060
478PhosphorylationATGPLPGTKVEPTLV
CCCCCCCCCCCCCEE
29.9428833060
483PhosphorylationPGTKVEPTLVDRNCP
CCCCCCCCEECCCCC
26.3826060331
491PhosphorylationLVDRNCPSPVLIDCP
EECCCCCCCEEEECC
29.8227087446
525PhosphorylationHAHTDDDSKPEADGD
ECCCCCCCCCCCCCC
58.0421183079
533PhosphorylationKPEADGDSEYGEEPA
CCCCCCCCCCCCCCC
37.9421183079
557PhosphorylationAPVPQKGSLSPARSA
CCCCCCCCCCCCCCC
32.4823984901
559PhosphorylationVPQKGSLSPARSATP
CCCCCCCCCCCCCCC
20.4327149854
563PhosphorylationGSLSPARSATPKVRL
CCCCCCCCCCCCEEE
38.3023984901
565PhosphorylationLSPARSATPKVRLVE
CCCCCCCCCCEEEEC
25.5326745281
575PhosphorylationVRLVEPHSPSPSSKF
EEEECCCCCCCCCCC
37.4827087446
577PhosphorylationLVEPHSPSPSSKFST
EECCCCCCCCCCCCC
40.1927087446
579PhosphorylationEPHSPSPSSKFSTKG
CCCCCCCCCCCCCCC
50.9621082442
580PhosphorylationPHSPSPSSKFSTKGL
CCCCCCCCCCCCCCC
40.9021082442
604PhosphorylationDTDPGALSNDGSDDG
CCCCCCCCCCCCCCC
32.1319854140
608PhosphorylationGALSNDGSDDGPSVM
CCCCCCCCCCCCCCC
35.0819854140
618PhosphorylationGPSVMDETSNDAFDS
CCCCCCCCCCHHHHH
28.6819854140
619PhosphorylationPSVMDETSNDAFDSL
CCCCCCCCCHHHHHH
30.5725338131
644PhosphorylationKKPSSLKSEKIPSKS
CCCCCCCCCCCCCCC
49.7925619855
649PhosphorylationLKSEKIPSKSLKSAR
CCCCCCCCCCCCCCC
38.0525619855
721PhosphorylationFTVNPALTPAKDKKK
CCCCCCCCCCCCCCC
24.2528066266
742PhosphorylationDSSKELESPLTPGKV
CCHHHCCCCCCCCCC
37.5228833060
745PhosphorylationKELESPLTPGKVCRA
HHCCCCCCCCCCEEC
33.1225521595
757PhosphorylationCRAEEGKSPFRDAAG
EECCCCCCCCCCCCC
39.8826824392
779PhosphorylationLLNGSSESHQSRLAS
HHCCCCHHHHHHHHH
28.8628059163
782PhosphorylationGSSESHQSRLASIKA
CCCHHHHHHHHHHHH
24.6828059163
803PhosphorylationSFTDNAPSPSIGGSS
EECCCCCCCCCCCCC
28.9525521595
805PhosphorylationTDNAPSPSIGGSSRL
CCCCCCCCCCCCCCC
37.9025619855
809PhosphorylationPSPSIGGSSRLDSTT
CCCCCCCCCCCCCCC
13.6825619855
810PhosphorylationSPSIGGSSRLDSTTP
CCCCCCCCCCCCCCC
39.8925619855
814PhosphorylationGGSSRLDSTTPTQPL
CCCCCCCCCCCCCCC
38.4826643407
815PhosphorylationGSSRLDSTTPTQPLT
CCCCCCCCCCCCCCC
36.1426643407
816PhosphorylationSSRLDSTTPTQPLTP
CCCCCCCCCCCCCCC
28.4326643407
818PhosphorylationRLDSTTPTQPLTPLH
CCCCCCCCCCCCCEE
40.5026643407
822PhosphorylationTTPTQPLTPLHVVTQ
CCCCCCCCCEEEEEC
30.4126643407
828PhosphorylationLTPLHVVTQNGAEAS
CCCEEEEECCCCCCC
18.4126643407
839PhosphorylationAEASSVKTNSPAYSD
CCCCCCCCCCCCCCC
38.4826745281
841PhosphorylationASSVKTNSPAYSDIS
CCCCCCCCCCCCCCC
19.0123684622
844PhosphorylationVKTNSPAYSDISDAG
CCCCCCCCCCCCCCC
15.4026643407
845PhosphorylationKTNSPAYSDISDAGE
CCCCCCCCCCCCCCC
30.4923684622
848PhosphorylationSPAYSDISDAGEDGE
CCCCCCCCCCCCCCC
26.8023684622
860PhosphorylationDGEGKVDSAKSKDPE
CCCCCCCCCCCCCHH
40.3523984901
871AcetylationKDPEQLVKEGAKKTL
CCHHHHHHHCCCCCC
60.0519855097
905PhosphorylationYSPGYAQSSPGTLTS
CCCCCCCCCCCCCCC
30.2626643407
906PhosphorylationSPGYAQSSPGTLTSS
CCCCCCCCCCCCCCC
18.4426643407
909PhosphorylationYAQSSPGTLTSSSQA
CCCCCCCCCCCCCCC
30.1926643407
911PhosphorylationQSSPGTLTSSSQAGM
CCCCCCCCCCCCCCC
26.8026643407
912PhosphorylationSSPGTLTSSSQAGME
CCCCCCCCCCCCCCC
30.9826643407
913PhosphorylationSPGTLTSSSQAGMEG
CCCCCCCCCCCCCCC
22.6426643407
914PhosphorylationPGTLTSSSQAGMEGQ
CCCCCCCCCCCCCCC
24.6626643407
1027PhosphorylationQRGLDKKTEMGLKER
HHCCHHHHHHHHHHH
36.6225619855
1037PhosphorylationGLKEREASLKEEWKQ
HHHHHHHHHHHHHHC
34.9125619855
1057PhosphorylationPTLTKAPSLTDLVKS
CCCCCCCCHHHHHHC
49.0825521595
1059PhosphorylationLTKAPSLTDLVKSGP
CCCCCCHHHHHHCCC
31.4628833060
1177AcetylationKEDRSRSKDSVPKED
HHHHHCCCCCCCCCC
53.57-
1287PhosphorylationDADKARASPSVSCKA
CHHHHHCCCCCCCCC
16.5030352176
1289PhosphorylationDKARASPSVSCKASS
HHHHCCCCCCCCCCC
24.9429472430
1291PhosphorylationARASPSVSCKASSES
HHCCCCCCCCCCCHH
17.7829472430
1311PhosphorylationLQQHASHYKSKSPTI
HHHHHHHHCCCCCCC
17.9221454597
1313PhosphorylationQHASHYKSKSPTISD
HHHHHHCCCCCCCCC
31.0625266776
1315PhosphorylationASHYKSKSPTISDKN
HHHHCCCCCCCCCCC
34.0726824392
1317PhosphorylationHYKSKSPTISDKNSQ
HHCCCCCCCCCCCCC
39.9628066266
1319PhosphorylationKSKSPTISDKNSQER
CCCCCCCCCCCCCCC
45.0428066266
1352PhosphorylationGAGGTDRSADRPRTS
CCCCCCCCCCCCCCC
37.01-

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 ZN609_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN609_MOUSE !!

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 ZN609_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN609_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN609_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575 AND SER-577, ANDMASS SPECTROMETRY.

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