ZC11A_MOUSE - dbPTM
ZC11A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZC11A_MOUSE
UniProt AC Q6NZF1
Protein Name Zinc finger CCCH domain-containing protein 11A
Gene Name Zc3h11a
Organism Mus musculus (Mouse).
Sequence Length 792
Subcellular Localization
Protein Description Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex..
Protein Sequence MPNQGEDCYFYFYSTCAKGDSCPFRHCEAALGNETVCTLWQEGRCFRQVCRFRHMEIDKKRSEIPCYWENQPVGCQKLNCAFHHTRSRYVDGLFLPPSKTVLPTVPESQEEEVKTSQLTVQQSKLSVQSNPSPQLRSVMKVESSENVPSPTHPPVVINAADDDEDDDDQFSEEGDESKTPALQPSPDVHNGLRVASARKPGVSLKQGECLNFGIKTLEEIKSKKMKEKSKKQGEGSSGVSSVLQQPQPNPGPEKENVRTVVRMVTLSSKPEEPLVRLSLSERLGKRKLSVGGDSDPPLKRSLAQRLGKKVESPETNIDKAPKKERGHKAGEIHVKTLEEILLERASQKRGELQTKLKAEEPSGADDSPSGTKSSSSVRIKTFSEVLAEKKHRQQEMERQKSKKDTSCLTLTDDTEMKKTVSLPTVAVSKGQPEEPAGRARSMQEVHIKTLEEIKLEKALRVQQSSESSGNSRPQAEAAPGTKRLLRITKRAGVKEEKKCGLEDSGDPPQSSVTKMEANETSDETISDPTKLAVNRCDTVKEKHTQRLQERGASQKEKAALSSVRGDEASSYTRVAGKPVLTAVSGVTRHLAKRLPVESSQKGEVETSGIGDSILNVKCAAQTLEKRSKVKPKVNVKPSVVKVVSAPKLAPKRKAVEMHSAVIAAVKPLSSSSVLQESPTKKAAVAVVPLLSEDKPVTMSETENPKDSSVLSSAQAASEPLLPEGSGPSSSQTATKPRRLSSASTGKPPLSVEDDFEKLIWEISGGKLEAEIDLDPGKDEDDLLLELSEMIDS
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
108PhosphorylationVLPTVPESQEEEVKT
CCCCCCHHHHHHHHH		36.5027841257
126PhosphorylationTVQQSKLSVQSNPSP
EEEHHHHHHCCCCCH		23.1128285833
129PhosphorylationQSKLSVQSNPSPQLR
HHHHHHCCCCCHHHH		48.8625619855
132PhosphorylationLSVQSNPSPQLRSVM
HHHCCCCCHHHHHEE		29.5426824392
143PhosphorylationRSVMKVESSENVPSP
HHEEEEECCCCCCCC		46.0325619855
144PhosphorylationSVMKVESSENVPSPT
HEEEEECCCCCCCCC		21.4925619855
149PhosphorylationESSENVPSPTHPPVV
ECCCCCCCCCCCCEE		37.8425521595
151PhosphorylationSENVPSPTHPPVVIN
CCCCCCCCCCCEEEE		51.8825619855
171PhosphorylationEDDDDQFSEEGDESK
CCCCCCCCCCCCCCC		29.1625521595
177PhosphorylationFSEEGDESKTPALQP
CCCCCCCCCCCCCCC		46.7125619855
179PhosphorylationEEGDESKTPALQPSP
CCCCCCCCCCCCCCC		24.0725367039
185PhosphorylationKTPALQPSPDVHNGL
CCCCCCCCCCCCCCE		22.2926824392
215AcetylationECLNFGIKTLEEIKS
CHHHHCCHHHHHHHH		47.6522826441
229PhosphorylationSKKMKEKSKKQGEGS
HHHHHHHHHHCCCCC		46.2925890499
259PhosphorylationPEKENVRTVVRMVTL
CCCCHHEEEEEEEEC		21.0423737553
265PhosphorylationRTVVRMVTLSSKPEE
EEEEEEEECCCCCCC		16.1623737553
267PhosphorylationVVRMVTLSSKPEEPL
EEEEEECCCCCCCCC		27.2723737553
268PhosphorylationVRMVTLSSKPEEPLV
EEEEECCCCCCCCCE		56.1723737553
280PhosphorylationPLVRLSLSERLGKRK
CCEEHHHHHHHCCCC		19.7924719451
289PhosphorylationRLGKRKLSVGGDSDP
HHCCCCCCCCCCCCH		23.0426824392
294PhosphorylationKLSVGGDSDPPLKRS
CCCCCCCCCHHHHHH		56.1223984901
312PhosphorylationRLGKKVESPETNIDK
HHCCCCCCCCCCCCC		30.9027087446
315PhosphorylationKKVESPETNIDKAPK
CCCCCCCCCCCCCCH		40.6425619855
346PhosphorylationEILLERASQKRGELQ
HHHHHHHHHHHCHHH		42.32-
362PhosphorylationKLKAEEPSGADDSPS
HHCCCCCCCCCCCCC		50.3125619855
367PhosphorylationEPSGADDSPSGTKSS
CCCCCCCCCCCCCCC		22.8525521595
369PhosphorylationSGADDSPSGTKSSSS
CCCCCCCCCCCCCCC		64.1525619855
371PhosphorylationADDSPSGTKSSSSVR
CCCCCCCCCCCCCEE		31.9025619855
380AcetylationSSSSVRIKTFSEVLA
CCCCEEEEEHHHHHH		32.7122826441
383PhosphorylationSVRIKTFSEVLAEKK
CEEEEEHHHHHHHHH		31.8429514104
389AcetylationFSEVLAEKKHRQQEM
HHHHHHHHHHHHHHH		48.5523806337
419PhosphorylationDDTEMKKTVSLPTVA
CCCHHCEEEECCEEE		15.1429176673
421PhosphorylationTEMKKTVSLPTVAVS
CHHCEEEECCEEEEC		33.5927841257
441PhosphorylationEPAGRARSMQEVHIK
CCCCCCCCCCEEECH		24.6729176673
464PhosphorylationKALRVQQSSESSGNS
HHHHHHCCCCCCCCC		20.9829899451
471PhosphorylationSSESSGNSRPQAEAA
CCCCCCCCCCHHHHC		49.19-
510PhosphorylationDSGDPPQSSVTKMEA
CCCCCCCCCCCEEEC		32.3325619855
511PhosphorylationSGDPPQSSVTKMEAN
CCCCCCCCCCEEECC		28.6725619855
513PhosphorylationDPPQSSVTKMEANET
CCCCCCCCEEECCCC		26.9925619855
520PhosphorylationTKMEANETSDETISD
CEEECCCCCCCCCCC		41.0821149613
521PhosphorylationKMEANETSDETISDP
EEECCCCCCCCCCCH		27.5421149613
524PhosphorylationANETSDETISDPTKL
CCCCCCCCCCCHHHH		30.6721149613
562PhosphorylationKEKAALSSVRGDEAS
HHHHHHHHHCCCCHH		19.3829514104
569PhosphorylationSVRGDEASSYTRVAG
HHCCCCHHHHHEECC		23.1025777480
570PhosphorylationVRGDEASSYTRVAGK
HCCCCHHHHHEECCC		37.2625777480
571PhosphorylationRGDEASSYTRVAGKP
CCCCHHHHHEECCCC		8.9625777480
572PhosphorylationGDEASSYTRVAGKPV
CCCHHHHHEECCCCC		22.1825777480
577AcetylationSYTRVAGKPVLTAVS
HHHEECCCCCEEHHH		23.4019863657
581PhosphorylationVAGKPVLTAVSGVTR
ECCCCCEEHHHHHHH		25.8325777480
584PhosphorylationKPVLTAVSGVTRHLA
CCCEEHHHHHHHHHH		25.6925777480
587PhosphorylationLTAVSGVTRHLAKRL
EEHHHHHHHHHHHHC		18.8522817900
641AcetylationNVKPSVVKVVSAPKL
CCCCEEEEEEECCCC		34.4622826441
644PhosphorylationPSVVKVVSAPKLAPK
CEEEEEEECCCCCCC		41.6727600695
659PhosphorylationRKAVEMHSAVIAAVK
CCHHHHHHHHHHHHC		23.9525777480
669PhosphorylationIAAVKPLSSSSVLQE
HHHHCCCCCCHHHCC		36.3825159016
670PhosphorylationAAVKPLSSSSVLQES
HHHCCCCCCHHHCCC		34.0225159016
671PhosphorylationAVKPLSSSSVLQESP
HHCCCCCCHHHCCCC		22.5325159016
672PhosphorylationVKPLSSSSVLQESPT
HCCCCCCHHHCCCCC		28.8825159016
677PhosphorylationSSSVLQESPTKKAAV
CCHHHCCCCCCCEEE		25.5526824392
679PhosphorylationSVLQESPTKKAAVAV
HHHCCCCCCCEEEEE		55.2322942356
691PhosphorylationVAVVPLLSEDKPVTM
EEEEECCCCCCCCCC		51.9729514104
717PhosphorylationLSSAQAASEPLLPEG
HHHHHHHCCCCCCCC		42.6425338131
740PhosphorylationATKPRRLSSASTGKP
CCCCCCCCCCCCCCC		23.2627087446
741PhosphorylationTKPRRLSSASTGKPP
CCCCCCCCCCCCCCC		30.7225521595
743PhosphorylationPRRLSSASTGKPPLS
CCCCCCCCCCCCCCC		39.3725521595
744PhosphorylationRRLSSASTGKPPLSV
CCCCCCCCCCCCCCC		49.2827087446
746AcetylationLSSASTGKPPLSVED
CCCCCCCCCCCCCHH		43.48-
750PhosphorylationSTGKPPLSVEDDFEK
CCCCCCCCCHHHHHH		29.2721082442
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 ZC11A_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZC11A_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 ZC11A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZC11A_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZC11A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741 AND THR-744, ANDMASS SPECTROMETRY.

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