ANKZ1_HUMAN - dbPTM
ANKZ1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANKZ1_HUMAN
UniProt AC Q9H8Y5
Protein Name Ankyrin repeat and zinc finger domain-containing protein 1
Gene Name ANKZF1
Organism Homo sapiens (Human).
Sequence Length 726
Subcellular Localization Cytoplasm . Translocates to the mitochondria upon exposure to hydrogen peroxide.
Protein Description Plays a role in the cellular response to hydrogen peroxide and in the maintenance of mitochondrial integrity under conditions of cellular stress. [PubMed: 28302725 Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway (By similarity]
Protein Sequence MSPAPDAAPAPASISLFDLSADAPVFQGLSLVSHAPGEALARAPRTSCSGSGERESPERKLLQGPMDISEKLFCSTCDQTFQNHQEQREHYKLDWHRFNLKQRLKDKPLLSALDFEKQSSTGDLSSISGSEDSDSASEEDLQTLDRERATFEKLSRPPGFYPHRVLFQNAQGQFLYAYRCVLGPHQDPPEEAELLLQNLQSRGPRDCVVLMAAAGHFAGAIFQGREVVTHKTFHRYTVRAKRGTAQGLRDARGGPSHSAGANLRRYNEATLYKDVRDLLAGPSWAKALEEAGTILLRAPRSGRSLFFGGKGAPLQRGDPRLWDIPLATRRPTFQELQRVLHKLTTLHVYEEDPREAVRLHSPQTHWKTVREERKKPTEEEIRKICRDEKEALGQNEESPKQGSGSEGEDGFQVELELVELTVGTLDLCESEVLPKRRRRKRNKKEKSRDQEAGAHRTLLQQTQEEEPSTQSSQAVAAPLGPLLDEAKAPGQPELWNALLAACRAGDVGVLKLQLAPSPADPRVLSLLSAPLGSGGFTLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTVAADKSTRNEFRRFMEKNPDAYDYNKAQVPGPLTPEMEARQATRKREQKAARRQREEQQQRQQEQEEREREEQRRFAALSDREKRALAAERRLAAQLGAPTSPIPDSAIVNTRRCWSCGASLQGLTPFHYLDFSFCSTRCLQDHRRQAGRPSS
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
2Phosphorylation------MSPAPDAAP
------CCCCCCCCC		29.7525159151
15PhosphorylationAPAPASISLFDLSAD
CCCCCEEEEEECCCC		22.0846164489
46PhosphorylationALARAPRTSCSGSGE
HHHCCCCCCCCCCCC		32.7868705089
47PhosphorylationLARAPRTSCSGSGER
HHCCCCCCCCCCCCC		13.9428985074
49PhosphorylationRAPRTSCSGSGERES
CCCCCCCCCCCCCCC		35.4468705101
51PhosphorylationPRTSCSGSGERESPE
CCCCCCCCCCCCCHH		22.6130576142
56PhosphorylationSGSGERESPERKLLQ
CCCCCCCCHHHHHHC		37.9825159151
66SulfoxidationRKLLQGPMDISEKLF
HHHHCCCCCHHHHHH		10.2621406390
75PhosphorylationISEKLFCSTCDQTFQ
HHHHHHCCCCHHHHH		25.4128555341
80PhosphorylationFCSTCDQTFQNHQEQ
HCCCCHHHHHHHHHH		17.5928555341
101MethylationDWHRFNLKQRLKDKP
CHHHCCHHHHHCCCC		34.18-
119PhosphorylationALDFEKQSSTGDLSS
HHCHHCCCCCCCHHH		40.7217081983
120PhosphorylationLDFEKQSSTGDLSSI
HCHHCCCCCCCHHHC		33.6417081983
121PhosphorylationDFEKQSSTGDLSSIS
CHHCCCCCCCHHHCC		39.7117081983
125PhosphorylationQSSTGDLSSISGSED
CCCCCCHHHCCCCCC		30.3022817900
126PhosphorylationSSTGDLSSISGSEDS
CCCCCHHHCCCCCCC		28.2422817900
128PhosphorylationTGDLSSISGSEDSDS
CCCHHHCCCCCCCCC		37.9122817900
130PhosphorylationDLSSISGSEDSDSAS
CHHHCCCCCCCCCCC		31.2922817900
133PhosphorylationSISGSEDSDSASEED
HCCCCCCCCCCCHHH		29.4322817900
135PhosphorylationSGSEDSDSASEEDLQ
CCCCCCCCCCHHHHH		37.3322817900
137PhosphorylationSEDSDSASEEDLQTL
CCCCCCCCHHHHHHH		45.5324461736
155PhosphorylationRATFEKLSRPPGFYP
HHHHHHHCCCCCCCC		54.5328555341
176PhosphorylationNAQGQFLYAYRCVLG
CCCCCEEEEEEHHHC		11.6883339
242MethylationRYTVRAKRGTAQGLR
EEEEECCCCCCCCCC		46.86-
252MethylationAQGLRDARGGPSHSA
CCCCCCCCCCCCCCC		55.69-
256PhosphorylationRDARGGPSHSAGANL
CCCCCCCCCCCCCHH		33.0920068231
258PhosphorylationARGGPSHSAGANLRR
CCCCCCCCCCCHHHH		32.5125159151
266PhosphorylationAGANLRRYNEATLYK
CCCHHHHCCHHHHHH		15.7722210691
273UbiquitinationYNEATLYKDVRDLLA
CCHHHHHHHHHHHHC		53.51-
286UbiquitinationLAGPSWAKALEEAGT
HCCHHHHHHHHHHCC		47.44-
301O-linked_GlycosylationILLRAPRSGRSLFFG
EEEECCCCCCCCCCC		37.1830379171
310UbiquitinationRSLFFGGKGAPLQRG
CCCCCCCCCCCCCCC		52.88-
310AcetylationRSLFFGGKGAPLQRG
CCCCCCCCCCCCCCC		52.8825953088
361PhosphorylationREAVRLHSPQTHWKT
HHHHHCCCCCCHHHH		24.2422167270
364PhosphorylationVRLHSPQTHWKTVRE
HHCCCCCCHHHHHHH		32.8430266825
367UbiquitinationHSPQTHWKTVREERK
CCCCCHHHHHHHHHC		29.54-
398PhosphorylationALGQNEESPKQGSGS
HHCCCCCCCCCCCCC		31.0830266825
462PhosphorylationHRTLLQQTQEEEPST
HHHHHHHHHCCCCCC		25.6128348404
511UbiquitinationAGDVGVLKLQLAPSP
CCCCEEEEEEECCCC		31.61-
517PhosphorylationLKLQLAPSPADPRVL
EEEEECCCCCCHHHH		27.4128674419
525PhosphorylationPADPRVLSLLSAPLG
CCCHHHHHHHCCCCC		25.1424732914
528PhosphorylationPRVLSLLSAPLGSGG
HHHHHHHCCCCCCCC		32.8824732914
533PhosphorylationLLSAPLGSGGFTLLH
HHCCCCCCCCHHHHH		43.3529255136
537PhosphorylationPLGSGGFTLLHAAAA
CCCCCCHHHHHHHHH		31.5229255136
562PhosphorylationLEAGADPTVQDSRAR
HHCCCCCCCCCCCCC		31.2020068231
566PhosphorylationADPTVQDSRARPPYT
CCCCCCCCCCCCCCE		15.6820068231
572PhosphorylationDSRARPPYTVAADKS
CCCCCCCCEEECCCH		19.2722817900
573PhosphorylationSRARPPYTVAADKST
CCCCCCCEEECCCHH		14.9429083192
579PhosphorylationYTVAADKSTRNEFRR
CEEECCCHHHHHHHH		32.9029083192
580PhosphorylationTVAADKSTRNEFRRF
EEECCCHHHHHHHHH		43.1629083192
599MethylationPDAYDYNKAQVPGPL
CCCCCCCCCCCCCCC		33.69-
607PhosphorylationAQVPGPLTPEMEARQ
CCCCCCCCHHHHHHH		21.9729255136
616PhosphorylationEMEARQATRKREQKA
HHHHHHHHHHHHHHH		28.5229514088
653PhosphorylationQRRFAALSDREKRAL
HHHHHHHCHHHHHHH		29.8721815630
674PhosphorylationAAQLGAPTSPIPDSA
HHHHCCCCCCCCCCC		46.7516964243
675PhosphorylationAQLGAPTSPIPDSAI
HHHCCCCCCCCCCCE		21.5530175587
680PhosphorylationPTSPIPDSAIVNTRR
CCCCCCCCCEECCCC		17.9727794612
685PhosphorylationPDSAIVNTRRCWSCG
CCCCEECCCCCCCCC		14.4830108239
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 ANKZ1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANKZ1_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 ANKZ1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
21896481
TERA_HUMANVCPphysical
21914798
A4_HUMANAPPphysical
21832049
NAA35_HUMANNAA35physical
26344197
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 ANKZ1_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-398; THR-607 ANDSER-675, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607 AND SER-675, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398 AND THR-607, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND MASSSPECTROMETRY.

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