ZN148_MOUSE - dbPTM
ZN148_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN148_MOUSE
UniProt AC Q61624
Protein Name Zinc finger protein 148
Gene Name Znf148
Organism Mus musculus (Mouse).
Sequence Length 794
Subcellular Localization Nucleus.
Protein Description Involved in transcriptional regulation. Represses the transcription of a number of genes including gastrin, stromelysin and enolase. Binds to the G-rich box in the enhancer region of these genes..
Protein Sequence MNIDDKLEGLFLKCGGIDEMQSSRAMVVMGGVSGQSAVSGELQESVLQDRSLPHQEILAADEVLQESEMRQQDMISHDELMVHEETVKNDEEQMDTHERLPQGLQYALNVPISVKQEITFTDVSEQLMRDKKQVREPVDLQKKKKRKQRSPAKILTINEDGSLGLKTPKSHVCEHCNAAFRTNYHLQRHVFIHTGEKPFQCSQCDMRFIQKYLLQRHEKIHTGEKPFRCDECGMRFIQKYHMERHKRTHSGEKPYQCEYCLQYFSRTDRVLKHKRMCHENHDKKLNRCAIKGGLLTSEEDSGFSTSPKDNSLPKKKRQKTEKKSSGMDKESVLDKSDLKKDKNDYLPLYSSSTKVKDEYMVAEYAVEMPHSSVGGSHLEDASGEIHPPKLVLKKINSKRSLKQPLEQSQTISPLSSYEDSKVSKYAFELVDKQALLDSEGSADIDQVDNLQEGPSKPVHSSTNYDDAMQFLKKKRYLQAASNNSREYALNVGTIASQPSVTQAAVASVIDESTTASILDSQALNVEIKSNHDKNVIPDEVLQTLLDHYSHKPNGQHEISFSVADTEVTSSISINSSDVPEVTQSENVGSSSQASSSDKANMLQEYSKFLQQALDRTSQNDAYLNSPSLNFVTDNQTLPNPPAFSSIDKQVYAAMPINSFRSGMNSPLRTTPDKSHFGLIVGDSQHPFPFSGDETNHASATSTADFLDQVTSQKKAEAQPVHQAYQMSSFEQPFRAPYHGSRAGIATQFSTANGQVNLRGPGTSAEFSEFPLVNVNDNRAGMTSSPDATTGQTFG
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
51PhosphorylationESVLQDRSLPHQEIL
HHHHCCCCCCHHHHH		55.3222817900
115SumoylationLNVPISVKQEITFTD
HCCCEEECEEEEECC		35.11-
150PhosphorylationKKKRKQRSPAKILTI
HHHHCCCCCCCEEEE		27.0722324799
162PhosphorylationLTINEDGSLGLKTPK
EEECCCCCCCCCCCC		31.4226643407
167PhosphorylationDGSLGLKTPKSHVCE
CCCCCCCCCCCHHHH		40.7826643407
194PhosphorylationQRHVFIHTGEKPFQC
CCCEEEECCCCCCCC		42.07-
222PhosphorylationQRHEKIHTGEKPFRC
HHHHCCCCCCCCCCC		50.97-
250PhosphorylationERHKRTHSGEKPYQC
HHHCCCCCCCCCCCC		48.29-
296PhosphorylationAIKGGLLTSEEDSGF
HEECCCCCCCCCCCC		38.8525619855
297PhosphorylationIKGGLLTSEEDSGFS
EECCCCCCCCCCCCC		38.6727742792
301PhosphorylationLLTSEEDSGFSTSPK
CCCCCCCCCCCCCCC		45.0427742792
304PhosphorylationSEEDSGFSTSPKDNS
CCCCCCCCCCCCCCC		31.3427087446
305PhosphorylationEEDSGFSTSPKDNSL
CCCCCCCCCCCCCCC		46.9527087446
306PhosphorylationEDSGFSTSPKDNSLP
CCCCCCCCCCCCCCC		28.8427087446
311PhosphorylationSTSPKDNSLPKKKRQ
CCCCCCCCCCHHHCH		57.0727742792
324PhosphorylationRQKTEKKSSGMDKES
CHHHCHHCCCCCHHH		43.1022418434
325PhosphorylationQKTEKKSSGMDKESV
HHHCHHCCCCCHHHH		47.2022418434
331PhosphorylationSSGMDKESVLDKSDL
CCCCCHHHHCCHHHH		33.4522418434
342AcetylationKSDLKKDKNDYLPLY
HHHHCCCCCCCCCCC		61.6723806337
356SumoylationYSSSTKVKDEYMVAE
CCCCCCCCCEEEEEE		46.53-
400PhosphorylationKKINSKRSLKQPLEQ
HHCCCCCCCCCCHHH		43.5925619855
408PhosphorylationLKQPLEQSQTISPLS
CCCCHHHCCCCCCCC		21.6625619855
410PhosphorylationQPLEQSQTISPLSSY
CCHHHCCCCCCCCCC		28.7722942356
412PhosphorylationLEQSQTISPLSSYED
HHHCCCCCCCCCCCC		24.1525521595
415PhosphorylationSQTISPLSSYEDSKV
CCCCCCCCCCCCHHH		33.9725619855
416PhosphorylationQTISPLSSYEDSKVS
CCCCCCCCCCCHHHH		39.9825619855
417PhosphorylationTISPLSSYEDSKVSK
CCCCCCCCCCHHHHH		22.0025619855
420PhosphorylationPLSSYEDSKVSKYAF
CCCCCCCHHHHHHHH		24.0225619855
438PhosphorylationDKQALLDSEGSADID
HHHHHHCCCCCCCHH		43.7729550500
441PhosphorylationALLDSEGSADIDQVD
HHHCCCCCCCHHHCC		20.7929550500
484PhosphorylationLQAASNNSREYALNV
HHHHHCCCCCEEECH		30.6422802335
493PhosphorylationEYALNVGTIASQPSV
CEEECHHHCCCCCCH		14.75-
607AcetylationNMLQEYSKFLQQALD
HHHHHHHHHHHHHHH		49.55-
625PhosphorylationQNDAYLNSPSLNFVT
CCCCCCCCCCCCCCC		17.1725338131
658PhosphorylationYAAMPINSFRSGMNS
HHCCCCCCCCCCCCC		23.8226643407
661PhosphorylationMPINSFRSGMNSPLR
CCCCCCCCCCCCCCC		40.1425521595
665PhosphorylationSFRSGMNSPLRTTPD
CCCCCCCCCCCCCCC		19.2025521595
669PhosphorylationGMNSPLRTTPDKSHF
CCCCCCCCCCCCCCC		50.8125521595
670PhosphorylationMNSPLRTTPDKSHFG
CCCCCCCCCCCCCCE		24.0527818261
728PhosphorylationHQAYQMSSFEQPFRA
HHHHHCCCCCCCCCC		27.7129899451
749PhosphorylationAGIATQFSTANGQVN
CEEEEEEECCCCEEE		19.4525266776
762PhosphorylationVNLRGPGTSAEFSEF
EEECCCCCCCCCCCC		28.0925338131
782PhosphorylationNDNRAGMTSSPDATT
CCCCCCCCCCCCCCC		25.7425619855
783PhosphorylationDNRAGMTSSPDATTG
CCCCCCCCCCCCCCC		30.8623527152
784PhosphorylationNRAGMTSSPDATTGQ
CCCCCCCCCCCCCCC		20.0325521595
788PhosphorylationMTSSPDATTGQTFG-
CCCCCCCCCCCCCC-		38.5525619855
789PhosphorylationTSSPDATTGQTFG--
CCCCCCCCCCCCC--		29.0725619855
792PhosphorylationPDATTGQTFG-----
CCCCCCCCCC-----		31.5025619855
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 ZN148_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN148_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 ZN148_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN148_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN148_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 THR-305 AND SER-306, ANDMASS SPECTROMETRY.

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