CCZ1B_HUMAN - dbPTM
CCZ1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCZ1B_HUMAN
UniProt AC P86790
Protein Name Vacuolar fusion protein CCZ1 homolog B
Gene Name CCZ1B
Organism Homo sapiens (Human).
Sequence Length 482
Subcellular Localization Lysosome membrane .
Protein Description
Protein Sequence MAAAAAGAGSGPWAAQEKQFPPALLSFFIYNPRFGPREGQEENKILFYHPNEVEKNEKIRNVGLCEAIVQFTRTFSPSKPAKSLHTQKNRQFFNEPEENFWMVMVVRNPIIEKQSKDGKPVIEYQEEELLDKVYSSVLRQCYSMYKLFNGTFLKAMEDGGVKLLKERLEKFFHRYLQTLHLQSCDLLDIFGGISFFPLDKMTYLKIQSFINRMEESLNIVKYTAFLYNDQLIWSGLEQDDMRILYKYLTTSLFPRHIEPELAGRDSPIRAEMPGNLQHYGRFLTGPLNLNDPDAKCRFPKIFVNTDDTYEELHLIVYKAMSAAVCFMIDASVHPTLDFCRRLDSIVGPQLTVLASDICEQFNINKRMSGSEKEPQFKFIYFNHMNLAEKSTVHMRKTPSVSLTSVHPDLMKILGDINSDFTRVDEDEEIIVKAMSDYWVVGKKSDRRELYVILNQKNANLIEVNEEVKKLCATQFNNIFFLD
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
2Acetylation------MAAAAAGAG
------CCCCCCCCC		13.0522223895
10PhosphorylationAAAAGAGSGPWAAQE
CCCCCCCCCHHHHHH		40.9425159151
44UbiquitinationREGQEENKILFYHPN
CCCCCCCCEEEECCC		44.03-
45UbiquitinationEGQEENKILFYHPNE
CCCCCCCEEEECCCH		4.9221890473
55UbiquitinationYHPNEVEKNEKIRNV
ECCCHHHCCHHHCCC		75.48-
74PhosphorylationAIVQFTRTFSPSKPA
HHHHHHHCCCCCCCC		25.9623927012
76PhosphorylationVQFTRTFSPSKPAKS
HHHHHCCCCCCCCCC		27.8723927012
78PhosphorylationFTRTFSPSKPAKSLH
HHHCCCCCCCCCCCC		50.5028985074
79UbiquitinationTRTFSPSKPAKSLHT
HHCCCCCCCCCCCCC		52.99-
82UbiquitinationFSPSKPAKSLHTQKN
CCCCCCCCCCCCHHC		63.18-
88UbiquitinationAKSLHTQKNRQFFNE
CCCCCCHHCHHHCCC		56.08-
89UbiquitinationKSLHTQKNRQFFNEP
CCCCCHHCHHHCCCC		32.9221890473
113UbiquitinationVRNPIIEKQSKDGKP
EECHHHCCCCCCCCC		49.84-
116UbiquitinationPIIEKQSKDGKPVIE
HHHCCCCCCCCCCEE		68.92-
117UbiquitinationIIEKQSKDGKPVIEY
HHCCCCCCCCCCEEE		75.4921890473
119UbiquitinationEKQSKDGKPVIEYQE
CCCCCCCCCCEEECH		46.36-
120UbiquitinationKQSKDGKPVIEYQEE
CCCCCCCCCEEECHH		37.5421890473
124PhosphorylationDGKPVIEYQEEELLD
CCCCCEEECHHHHHH		15.3129496907
132UbiquitinationQEEELLDKVYSSVLR
CHHHHHHHHHHHHHH		42.94-
134PhosphorylationEELLDKVYSSVLRQC
HHHHHHHHHHHHHHH		10.8529496907
136PhosphorylationLLDKVYSSVLRQCYS
HHHHHHHHHHHHHHH		13.90-
142PhosphorylationSSVLRQCYSMYKLFN
HHHHHHHHHHHHHHC		6.53-
143PhosphorylationSVLRQCYSMYKLFNG
HHHHHHHHHHHHHCC		24.22-
145PhosphorylationLRQCYSMYKLFNGTF
HHHHHHHHHHHCCCH		9.90-
162UbiquitinationAMEDGGVKLLKERLE
HHHHCCHHHHHHHHH		51.91-
170AcetylationLLKERLEKFFHRYLQ
HHHHHHHHHHHHHHH		58.9019608861
216PhosphorylationFINRMEESLNIVKYT
HHHHHHHHHCHHHHH		17.26-
246UbiquitinationDDMRILYKYLTTSLF
HHHHHHHHHHHHHCC		30.27-
247PhosphorylationDMRILYKYLTTSLFP
HHHHHHHHHHHHCCC		8.8424114839
247UbiquitinationDMRILYKYLTTSLFP
HHHHHHHHHHHHCCC		8.8421890473
266PhosphorylationPELAGRDSPIRAEMP
HHHCCCCCCCCCCCC		22.3629255136
266PhosphorylationPELAGRDSPIRAEMP
HHHCCCCCCCCCCCC		22.3618669648
279PhosphorylationMPGNLQHYGRFLTGP
CCCCHHCCCCCCCCC		9.3129978859
295AcetylationNLNDPDAKCRFPKIF
CCCCCCCCCCCCEEE		33.0725953088
295UbiquitinationNLNDPDAKCRFPKIF
CCCCCCCCCCCCEEE		33.07-
368PhosphorylationFNINKRMSGSEKEPQ
CCCCCCCCCCCCCCC		43.1126657352
370PhosphorylationINKRMSGSEKEPQFK
CCCCCCCCCCCCCCE		37.8820068231
372AcetylationKRMSGSEKEPQFKFI
CCCCCCCCCCCCEEE		76.1225953088
372UbiquitinationKRMSGSEKEPQFKFI
CCCCCCCCCCCCEEE		76.12-
373UbiquitinationRMSGSEKEPQFKFIY
CCCCCCCCCCCEEEE		40.0421890473
380PhosphorylationEPQFKFIYFNHMNLA
CCCCEEEEEECCCHH		11.0628152594
389UbiquitinationNHMNLAEKSTVHMRK
ECCCHHHHCCEECCC		45.91-
396UbiquitinationKSTVHMRKTPSVSLT
HCCEECCCCCCCEEE		58.16-
397PhosphorylationSTVHMRKTPSVSLTS
CCEECCCCCCCEEEE		15.4929978859
399PhosphorylationVHMRKTPSVSLTSVH
EECCCCCCCEEEECC		29.5729978859
401PhosphorylationMRKTPSVSLTSVHPD
CCCCCCCEEEECCHH		30.2123186163
403PhosphorylationKTPSVSLTSVHPDLM
CCCCCEEEECCHHHH		22.6123186163
404PhosphorylationTPSVSLTSVHPDLMK
CCCCEEEECCHHHHH		24.5823186163
411UbiquitinationSVHPDLMKILGDINS
ECCHHHHHHHCCCCC		41.92-
435PhosphorylationEIIVKAMSDYWVVGK
HHHHHHHCCEEEEEE		32.2028796482
437PhosphorylationIVKAMSDYWVVGKKS
HHHHHCCEEEEEECC		7.8728796482
442UbiquitinationSDYWVVGKKSDRREL
CCEEEEEECCCCCEE		37.18-
443UbiquitinationDYWVVGKKSDRRELY
CEEEEEECCCCCEEE		52.22-
450PhosphorylationKSDRRELYVILNQKN
CCCCCEEEEEEECCC		4.8227642862
456UbiquitinationLYVILNQKNANLIEV
EEEEEECCCCCEEEC		57.88-
468UbiquitinationIEVNEEVKKLCATQF
EECCHHHHHHHHHHC		43.22-
469UbiquitinationEVNEEVKKLCATQFN
ECCHHHHHHHHHHCC		54.71-
469UbiquitinationEVNEEVKKLCATQFN
ECCHHHHHHHHHHCC		54.7121890473
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 CCZ1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCZ1B_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 CCZ1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CCZ1B_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CCZ1B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-170, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-266, AND MASSSPECTROMETRY.
"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-266, AND MASSSPECTROMETRY.

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