ZCH14_HUMAN - dbPTM
ZCH14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZCH14_HUMAN
UniProt AC Q8WYQ9
Protein Name Zinc finger CCHC domain-containing protein 14
Gene Name ZCCHC14
Organism Homo sapiens (Human).
Sequence Length 949
Subcellular Localization
Protein Description
Protein Sequence MASNHPAFSFHQKQVLRQELTQIQSSLNGGGGHGGKGAPGPGGALPTCPACHKITPRTEAPVSSVSNSLENALHTSAHSTEESLPKRPLGKHSKVSVEKIDLKGLSHTKNDRNVECSFEVLWSDSSITSVTKSSSEVTEFISKLCQLYPEENLEKLIPCLAGPDAFYVERNHVDLDSGLRYLASLPSHVLKNDHVRRFLSTSSPPQQLQSPSPGNPSLSKVGTVMGVSGRPVCGVAGIPSSQSGAQHHGQHPAGSAAPLPHCSHAGSAGSALAYRTQMDTSPAILMPSSLQTPQTQEQNGILDWLRKLRLHKYYPVFKQLSMEKFLSLTEEDLNKFESLTMGAKKKLKTQLELEKEKSERRCLNPSAPPLVTSSGVARVPPTSHVGPVQSGRGSHAAELRVEVEQPHHQLPREGSSSEYSSSSSSPMGVQAREESSDSAEENDRRVEIHLESSDKEKPVMLLNHFTSSSARPTAQVLPVQNEASSNPSGHHPLPPQMLSAASHITPIRMLNSVHKPERGSADMKLLSSSVHSLLSLEERNKGSGPRSSMKVDKSFGSAMMDVLPASAPHQPVQVLSGLSESSSMSPTVSFGPRTKVVHASTLDRVLKTAQQPALVVETSTAATGTPSTVLHAARPPIKLLLSSSVPADSAISGQTSCPNNVQISVPPAIINPRTALYTANTKVAFSAMSSMPVGPLQGGFCANSNTASPSSHPSTSFANMATLPSCPAPSSSPALSSVPESSFYSSSGGGGSTGNIPASNPNHHHHHHHQQPPAPPQPAPPPPGCIVCTSCGCSGSCGSSGLTVSYANYFQHPFSGPSVFTFPFLPFSPMCSSGYVSAQQYGGGSTFPVVHAPYSSSGTPDPVLSGQSTFAVPPMQNFMAGTAGVYQTQGLVGSSNGSSHKKSGNLSCYNCGATGHRAQDCKQPSMDFNRPGTFRLKYAPPAESLDSTD
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
3Phosphorylation-----MASNHPAFSF
-----CCCCCCCCCH		34.0818187866
53UbiquitinationPTCPACHKITPRTEA
CCCCCCCCCCCCCCC		48.4329967540
108PhosphorylationDLKGLSHTKNDRNVE
ECCCCCCCCCCCCCE		28.3224719451
131PhosphorylationDSSITSVTKSSSEVT
CCCCEEEECCHHHHH		25.61-
135PhosphorylationTSVTKSSSEVTEFIS
EEEECCHHHHHHHHH		43.08-
143UbiquitinationEVTEFISKLCQLYPE
HHHHHHHHHHHHCCH		48.7629967540
200PhosphorylationDHVRRFLSTSSPPQQ
HHHHHHHCCCCCCHH		24.4329978859
201PhosphorylationHVRRFLSTSSPPQQL
HHHHHHCCCCCCHHH		35.0629978859
202PhosphorylationVRRFLSTSSPPQQLQ
HHHHHCCCCCCHHHC		37.1530624053
203PhosphorylationRRFLSTSSPPQQLQS
HHHHCCCCCCHHHCC		40.4630624053
210PhosphorylationSPPQQLQSPSPGNPS
CCCHHHCCCCCCCCC		35.6225159151
212PhosphorylationPQQLQSPSPGNPSLS
CHHHCCCCCCCCCHH		51.1629978859
217PhosphorylationSPSPGNPSLSKVGTV
CCCCCCCCHHHCCEE		49.6429978859
321PhosphorylationYPVFKQLSMEKFLSL
HHHHHHHCHHHHHCC		23.5419413330
324AcetylationFKQLSMEKFLSLTEE
HHHHCHHHHHCCCHH		42.8590773
327PhosphorylationLSMEKFLSLTEEDLN
HCHHHHHCCCHHHHH		36.0619413330
355AcetylationKTQLELEKEKSERRC
HHHHHHHHHHHHHHC		80.9820167786
372O-linked_GlycosylationPSAPPLVTSSGVARV
CCCCCCCCCCCCCCC		25.5128657654
394PhosphorylationPVQSGRGSHAAELRV
CCCCCCCCCEEEEEE		14.4828555341
415PhosphorylationHQLPREGSSSEYSSS
CCCCCCCCCCCCCCC		26.4127732954
416PhosphorylationQLPREGSSSEYSSSS
CCCCCCCCCCCCCCC		37.7427732954
417PhosphorylationLPREGSSSEYSSSSS
CCCCCCCCCCCCCCC		42.1027732954
420PhosphorylationEGSSSEYSSSSSSPM
CCCCCCCCCCCCCCC		21.4927732954
421PhosphorylationGSSSEYSSSSSSPMG
CCCCCCCCCCCCCCC		33.0827732954
422PhosphorylationSSSEYSSSSSSPMGV
CCCCCCCCCCCCCCC		28.4427732954
423PhosphorylationSSEYSSSSSSPMGVQ
CCCCCCCCCCCCCCE		36.4627732954
424PhosphorylationSEYSSSSSSPMGVQA
CCCCCCCCCCCCCEE		40.1727732954
425PhosphorylationEYSSSSSSPMGVQAR
CCCCCCCCCCCCEEC		22.3627732954
520PhosphorylationVHKPERGSADMKLLS
CCCCCCCCCCHHHHH		27.5823917254
548PhosphorylationKGSGPRSSMKVDKSF
CCCCCCHHCEECHHH		24.7327251275
595UbiquitinationVSFGPRTKVVHASTL
EECCCCCEEEEHHHH		43.4729967540
608PhosphorylationTLDRVLKTAQQPALV
HHHHHHHHCCCCEEE		26.0728348404
903PhosphorylationNGSSHKKSGNLSCYN
CCCCCCCCCCEEEEC		37.4024114839
914PhosphorylationSCYNCGATGHRAQDC
EEECCCCCCCCCCCC		20.8524114839
937UbiquitinationRPGTFRLKYAPPAES
CCCEEECEECCCHHH		34.8029967540
948PhosphorylationPAESLDSTD------
CHHHCCCCC------		45.4528985074
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 ZCH14_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZCH14_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 ZCH14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZCH14_HUMAN !!
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 ZCH14_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321 AND SER-327, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.

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