CCZ1_HUMAN - dbPTM
CCZ1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCZ1_HUMAN
UniProt AC P86791
Protein Name Vacuolar fusion protein CCZ1 homolog
Gene Name CCZ1
Organism Homo sapiens (Human).
Sequence Length 482
Subcellular Localization Lysosome membrane .
Protein Description Acts in concert with MON1A, as a guanine exchange factor (GEF) for RAB7, promotes the exchange of GDP to GTP, converting it from an inactive GDP-bound form into an active GTP-bound form. [PubMed: 23084991]
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		13.0519413330
10PhosphorylationAAAAGAGSGPWAAQE
CCCCCCCCCHHHHHH		40.9425159151
44UbiquitinationREGQEENKILFYHPN
CCCCCCCCEEEECCC		44.0321906983
55UbiquitinationYHPNEVEKNEKIRNV
ECCCHHHCCHHHCCC		75.4829967540
74PhosphorylationAIVQFTRTFSPSKPA
HHHHHHHCCCCCCCC		25.9623927012
76PhosphorylationVQFTRTFSPSKPAKS
HHHHHCCCCCCCCCC		27.8723927012
78PhosphorylationFTRTFSPSKPAKSLH
HHHCCCCCCCCCCCC		50.5028985074
79UbiquitinationTRTFSPSKPAKSLHT
HHCCCCCCCCCCCCC		52.9927667366
82UbiquitinationFSPSKPAKSLHTQKN
CCCCCCCCCCCCHHC		63.1827667366
88UbiquitinationAKSLHTQKNRQFFNE
CCCCCCHHCHHHCCC		56.0821906983
113UbiquitinationVRNPIIEKQSKDGKP
EECHHHCCCCCCCCC		49.8421906983
116UbiquitinationPIIEKQSKDGKPVIE
HHHCCCCCCCCCCEE		68.9222817900
119UbiquitinationEKQSKDGKPVIEYQE
CCCCCCCCCCEEECH		46.3621906983
124PhosphorylationDGKPVIEYQEEELLD
CCCCCEEECHHHHHH		15.3129496907
132UbiquitinationQEEELLDKVYSSVLR
CHHHHHHHHHHHHHH		42.9429967540
134PhosphorylationEELLDKVYSSVLRQC
HHHHHHHHHHHHHHH		10.8529496907
136PhosphorylationLLDKVYSSVLRQCYS
HHHHHHHHHHHHHHH		13.90-
142PhosphorylationSSVLRQCYSMYKLFN
HHHHHHHHHHHHHHC		6.53-
143PhosphorylationSVLRQCYSMYKLFNG
HHHHHHHHHHHHHCC		24.22-
145PhosphorylationLRQCYSMYKLFNGTF
HHHHHHHHHHHCCCH		9.90-
162UbiquitinationAMEDGGVKLLKERLE
HHHHCCHHHHHHHHH		51.9122817900
165UbiquitinationDGGVKLLKERLEKFF
HCCHHHHHHHHHHHH		51.7522817900
170AcetylationLLKERLEKFFHRYLQ
HHHHHHHHHHHHHHH		58.9022645009
216PhosphorylationFINRMEESLNIVKYT
HHHHHHHHHCHHHHH		17.26-
246UbiquitinationDDMRILYKYLTTSLF
HHHHHHHHHHHHHCC		30.2721890473
247PhosphorylationDMRILYKYLTTSLFP
HHHHHHHHHHHHCCC		8.8424114839
266PhosphorylationPELAGRDSPIRAEMP
HHHCCCCCCCCCCCC		22.3629255136
279PhosphorylationMPGNLQHYGRFLTGP
CCCCHHCCCCCCCCC		9.3129978859
295UbiquitinationNLNDPDAKCRFPKIF
CCCCCCCCCCCCEEE		33.0723000965
300UbiquitinationDAKCRFPKIFVNTDD
CCCCCCCEEEECCCC		46.1723000965
368PhosphorylationFNINKRMSGSEKEPQ
CCCCCCCCCCCCCCC		43.1126657352
370PhosphorylationINKRMSGSEKEPQFK
CCCCCCCCCCCCCCE		37.8820068231
372UbiquitinationKRMSGSEKEPQFKFI
CCCCCCCCCCCCEEE		76.1221906983
380PhosphorylationEPQFKFIYFNHMNLA
CCCCEEEEEECCCHH		11.0628152594
389UbiquitinationNHMNLAEKSTVHMRK
ECCCHHHHCCEECCC		45.9129967540
396UbiquitinationKSTVHMRKTPSVSLT
HCCEECCCCCCCEEE		58.1623000965
397PhosphorylationSTVHMRKTPSVSLTS
CCEECCCCCCCEEEE		15.4929978859
399PhosphorylationVHMRKTPSVSLTSVH
EECCCCCCCEEEECC		29.5729978859
401PhosphorylationMRKTPSVSLTSVHPD
CCCCCCCEEEECCHH		30.2123186163
403PhosphorylationKTPSVSLTSVHPDLM
CCCCCEEEECCHHHH		22.6123186163
404PhosphorylationTPSVSLTSVHPDLMK
CCCCEEEECCHHHHH		24.5823186163
411UbiquitinationSVHPDLMKILGDINS
ECCHHHHHHHCCCCC		41.9229967540
435PhosphorylationEIIVKAMSDYWVVGK
HHHHHHHCCEEEEEE		32.2028796482
437PhosphorylationIVKAMSDYWVVGKKS
HHHHHCCEEEEEECC		7.8728796482
442UbiquitinationSDYWVVGKKSDRREL
CCEEEEEECCCCCEE		37.1829967540
468UbiquitinationIEVNEEVKKLCATQF
EECCHHHHHHHHHHC		43.2222817900
469UbiquitinationEVNEEVKKLCATQFN
ECCHHHHHHHHHHCC		54.7121963094
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 CCZ1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCZ1_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 CCZ1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CCZ1_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 CCZ1_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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