CASP7_HUMAN - dbPTM
CASP7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CASP7_HUMAN
UniProt AC P55210
Protein Name Caspase-7
Gene Name CASP7
Organism Homo sapiens (Human).
Sequence Length 303
Subcellular Localization Cytoplasm.
Protein Description Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death..
Protein Sequence MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ
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------MADDQGCIE
------CCCCCCCCC		29.1422223895
16PhosphorylationEEQGVEDSANEDSVD
CCCCCCCCCCCCCCC		21.3529255136
21PhosphorylationEDSANEDSVDAKPDR
CCCCCCCCCCCCCCH		18.7322167270
29PhosphorylationVDAKPDRSSFVPSLF
CCCCCCHHHCHHHHC		35.1925159151
30PhosphorylationDAKPDRSSFVPSLFS
CCCCCHHHCHHHHCC		31.0221815630
34PhosphorylationDRSSFVPSLFSKKKK
CHHHCHHHHCCCCCC		36.4222617229
37PhosphorylationSFVPSLFSKKKKNVT
HCHHHHCCCCCCCCE		49.1928355574
38AcetylationFVPSLFSKKKKNVTM
CHHHHCCCCCCCCEE		62.3725953088
38UbiquitinationFVPSLFSKKKKNVTM
CHHHHCCCCCCCCEE		62.37-
38MethylationFVPSLFSKKKKNVTM
CHHHHCCCCCCCCEE		62.37-
38 (in isoform 2)Ubiquitination-62.37-
39UbiquitinationVPSLFSKKKKNVTMR
HHHHCCCCCCCCEEC		68.71-
39 (in isoform 2)Ubiquitination-68.71-
44PhosphorylationSKKKKNVTMRSIKTT
CCCCCCCEECCEECC		19.0929514088
47PhosphorylationKKNVTMRSIKTTRDR
CCCCEECCEECCHHC		20.0225159151
50PhosphorylationVTMRSIKTTRDRVPT
CEECCEECCHHCCCC		25.9523909892
51PhosphorylationTMRSIKTTRDRVPTY
EECCEECCHHCCCCE		26.1023909892
58PhosphorylationTRDRVPTYQYNMNFE
CHHCCCCEECCCCHH		11.7020068231
60PhosphorylationDRVPTYQYNMNFEKL
HCCCCEECCCCHHHC		13.1320068231
69UbiquitinationMNFEKLGKCIIINNK
CCHHHCCCEEEECCC		32.47-
70 (in isoform 3)Phosphorylation-2.2827251275
80AcetylationINNKNFDKVTGMGVR
ECCCCCCCCCCCCCC		37.2425953088
80 (in isoform 2)Ubiquitination-37.24-
80UbiquitinationINNKNFDKVTGMGVR
ECCCCCCCCCCCCCC		37.24-
92UbiquitinationGVRNGTDKDAEALFK
CCCCCCHHHHHHHHH		59.69-
99UbiquitinationKDAEALFKCFRSLGF
HHHHHHHHHHHHCCC		33.06-
125 (in isoform 2)Ubiquitination-58.05-
125UbiquitinationKMQDLLKKASEEDHT
HHHHHHHHHCCCCHH		58.05-
132PhosphorylationKASEEDHTNAACFAC
HHCCCCHHHHHHHHH		38.5827251275
132 (in isoform 3)Ubiquitination-38.58-
153UbiquitinationEENVIYGKDGVTPIK
CCCEEECCCCCCCHH		34.05-
157PhosphorylationIYGKDGVTPIKDLTA
EECCCCCCCHHHHHH		25.4821815630
160UbiquitinationKDGVTPIKDLTAHFR
CCCCCCHHHHHHHHC		48.14-
160AcetylationKDGVTPIKDLTAHFR
CCCCCCHHHHHHHHC		48.1425953088
172UbiquitinationHFRGDRCKTLLEKPK
HHCCHHHHHHHHCCC		43.00-
173PhosphorylationFRGDRCKTLLEKPKL
HCCHHHHHHHHCCCE		39.9521555521
177UbiquitinationRCKTLLEKPKLFFIQ
HHHHHHHCCCEEEEE		47.63-
193 (in isoform 2)Phosphorylation-69.58-
193 (in isoform 3)Ubiquitination-69.58-
199PhosphorylationDDGIQADSGPINDTD
CCCCCCCCCCCCCCC		49.8628348404
200 (in isoform 2)Phosphorylation-27.88-
205 (in isoform 3)Ubiquitination-32.30-
234PhosphorylationPGYYSWRSPGRGSWF
CCCCCCCCCCCCHHH		26.0025159151
239PhosphorylationWRSPGRGSWFVQALC
CCCCCCCHHHHHHHH		18.9121555521
286UbiquitinationDPHFHEKKQIPCVVS
CCCCCHHCHHCHHHH		50.94-
319Phosphorylation-----------------------
-----------------------		27251275
319 (in isoform 3)Ubiquitination--
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
30SPhosphorylationKinasePAK2Q13177
PSP
173TPhosphorylationKinasePAK2Q13177
PSP
239SPhosphorylationKinasePAK2Q13177
PSP
-KUbiquitinationE3 ubiquitin ligaseBIRC2Q13490
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseBIRC3Q13489
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseXIAPP98170
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CASP7_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 CASP7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CASP2_HUMANCASP2physical
11399776
TNR1A_HUMANTNFRSF1Aphysical
11755217
XIAP_HUMANXIAPphysical
9230442
CSN6_HUMANCOPS6physical
17337451
BIRC6_HUMANBIRC6physical
15507451
XIAP_HUMANXIAPphysical
11257231
XIAP_HUMANXIAPphysical
11257230
XIAP_HUMANXIAPphysical
14512414
XIAP_HUMANXIAPphysical
9525868
SP1_HUMANSP1physical
10103059
RB_HUMANRB1physical
15735701
RB_HUMANRB1physical
11420704
PARP1_HUMANPARP1physical
9875225
CLSPN_HUMANCLSPNphysical
16123041
TEBP_HUMANPTGES3physical
18723680
GDIR1_HUMANARHGDIAphysical
18723680
PARP1_HUMANPARP1physical
18723680
VIME_HUMANVIMphysical
18723680
SPTN1_HUMANSPTAN1physical
18723680
STAT1_HUMANSTAT1physical
18723680
DFFA_HUMANDFFAphysical
18723680
ROCK1_HUMANROCK1physical
18723680
CASP7_HUMANCASP7physical
18723680
CASP9_HUMANCASP9physical
18723680
IF4H_HUMANEIF4Hphysical
22863883
GBP2_HUMANGBP2physical
22863883
PSF2_HUMANGINS2physical
22863883
MVD1_HUMANMVDphysical
22863883
KS6A1_HUMANRPS6KA1physical
22863883
CRYAB_HUMANCRYABphysical
23074197
XIAP_HUMANXIAPphysical
23074197
CRYAB_HUMANCRYABphysical
23049853
TEBP_HUMANPTGES3physical
22451931
PARP1_HUMANPARP1physical
22451931
SAT1_HUMANSAT1physical
25416956
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 CASP7_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-16, AND MASS SPECTROMETRY.
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-16, AND MASS SPECTROMETRY.

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