CATZ_HUMAN - dbPTM
CATZ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CATZ_HUMAN
UniProt AC Q9UBR2
Protein Name Cathepsin Z
Gene Name CTSZ
Organism Homo sapiens (Human).
Sequence Length 303
Subcellular Localization Lysosome.
Protein Description Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity..
Protein Sequence MARRGPGWRPLLLLVLLAGAAQGGLYFRRGQTCYRPLRGDGLAPLGRSTYPRPHEYLSPADLPKSWDWRNVDGVNYASITRNQHIPQYCGSCWAHASTSAMADRINIKRKGAWPSTLLSVQNVIDCGNAGSCEGGNDLSVWDYAHQHGIPDETCNNYQAKDQECDKFNQCGTCNEFKECHAIRNYTLWRVGDYGSLSGREKMMAEIYANGPISCGIMATERLANYTGGIYAEYQDTTYINHVVSVAGWGISDGTEYWIVRNSWGEPWGERGWLRIVTSTYKDGKGARYNLAIEEHCTFGDPIV
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
65PhosphorylationSPADLPKSWDWRNVD
CHHHCCCCCCCCCCC		28.4729759185
76PhosphorylationRNVDGVNYASITRNQ
CCCCCCCCCEEECCC		10.1829759185
78PhosphorylationVDGVNYASITRNQHI
CCCCCCCEEECCCCC		17.7128152594
80PhosphorylationGVNYASITRNQHIPQ
CCCCCEEECCCCCCC		22.5228152594
166AcetylationAKDQECDKFNQCGTC
HCCCCCCCCCCCCCC		58.8526051181
166UbiquitinationAKDQECDKFNQCGTC
HCCCCCCCCCCCCCC		58.8521963094
177AcetylationCGTCNEFKECHAIRN
CCCCHHHHHHEEEEC		53.9326051181
177UbiquitinationCGTCNEFKECHAIRN
CCCCHHHHHHEEEEC		53.9321963094
184N-linked_GlycosylationKECHAIRNYTLWRVG
HHHEEEECEEEEEEC		28.2019159218
193PhosphorylationTLWRVGDYGSLSGRE
EEEEECCCCCCCCHH		11.5921406692
195PhosphorylationWRVGDYGSLSGREKM
EEECCCCCCCCHHHH		17.0921406692
197PhosphorylationVGDYGSLSGREKMMA
ECCCCCCCCHHHHHH		37.1921406692
224N-linked_GlycosylationMATERLANYTGGIYA
ECHHHHHHHCCCEEE		39.22UniProtKB CARBOHYD
224N-linked_GlycosylationMATERLANYTGGIYA
ECHHHHHHHCCCEEE		39.2216399764
225PhosphorylationATERLANYTGGIYAE
CHHHHHHHCCCEEEE		10.9324043423
226PhosphorylationTERLANYTGGIYAEY
HHHHHHHCCCEEEEE		28.8324043423
230PhosphorylationANYTGGIYAEYQDTT
HHHCCCEEEEEECCC		9.1724043423
233PhosphorylationTGGIYAEYQDTTYIN
CCCEEEEEECCCEEE		11.9724043423
236PhosphorylationIYAEYQDTTYINHVV
EEEEEECCCEEEEEE		13.1324043423
237PhosphorylationYAEYQDTTYINHVVS
EEEEECCCEEEEEEE		30.6024043423
238PhosphorylationAEYQDTTYINHVVSV
EEEECCCEEEEEEEE		11.2124043423
244PhosphorylationTYINHVVSVAGWGIS
CEEEEEEEEEEECCC		12.7424043423
251PhosphorylationSVAGWGISDGTEYWI
EEEEECCCCCCEEEE		26.5024043423
254PhosphorylationGWGISDGTEYWIVRN
EECCCCCCEEEEEEC		30.7824043423
256PhosphorylationGISDGTEYWIVRNSW
CCCCCCEEEEEECCC		10.5624043423
277PhosphorylationRGWLRIVTSTYKDGK
CCEEEEEEEEEECCC		16.9928152594
278PhosphorylationGWLRIVTSTYKDGKG
CEEEEEEEEEECCCC		20.8828152594
279PhosphorylationWLRIVTSTYKDGKGA
EEEEEEEEEECCCCC		25.8128152594
280PhosphorylationLRIVTSTYKDGKGAR
EEEEEEEEECCCCCE		13.5728152594
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 CATZ_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CATZ_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 CATZ_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KRA59_HUMANKRTAP5-9physical
25416956
PLS1_HUMANPLSCR1physical
25416956
TRIM1_HUMANMID2physical
25416956
MTUS2_HUMANMTUS2physical
25416956
K1C40_HUMANKRT40physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
KRA59_HUMANKRTAP5-9physical
21516116
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 CATZ_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184, AND MASSSPECTROMETRY.

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