CASP2_HUMAN - dbPTM
CASP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CASP2_HUMAN
UniProt AC P42575
Protein Name Caspase-2
Gene Name CASP2
Organism Homo sapiens (Human).
Sequence Length 452
Subcellular Localization
Protein Description Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival..
Protein Sequence MAAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT
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------MAAPSAGSW
------CCCCCCCCC		28.2519413330
5Phosphorylation---MAAPSAGSWSTF
---CCCCCCCCCCHH		40.3028122231
8PhosphorylationMAAPSAGSWSTFQHK
CCCCCCCCCCHHHHH		19.9825159151
10PhosphorylationAPSAGSWSTFQHKEL
CCCCCCCCHHHHHHH		22.5028122231
15UbiquitinationSWSTFQHKELMAADR
CCCHHHHHHHHHHHH		41.58-
22MethylationKELMAADRGRRILGV
HHHHHHHHCCHHHHH		35.47-
41UbiquitinationPHHQETLKKNRVVLA
HHHHHHHHHCHHHHH		56.26-
42UbiquitinationHHQETLKKNRVVLAK
HHHHHHHHCHHHHHH		53.77-
46 (in isoform 2)Ubiquitination-3.7721906983
62 (in isoform 2)Ubiquitination-55.8521906983
67PhosphorylationLLEKDIITLEMRELI
HHHCCCCCHHHHHHH		19.5920068231
77SumoylationMRELIQAKVGSFSQN
HHHHHHHHHCCCHHC		30.65-
77UbiquitinationMRELIQAKVGSFSQN
HHHHHHHHHCCCHHC		30.6521906983
77 (in isoform 1)Ubiquitination-30.6521906983
77SumoylationMRELIQAKVGSFSQN
HHHHHHHHHCCCHHC		30.65-
93 (in isoform 1)Ubiquitination-70.7021906983
93UbiquitinationELLNLLPKRGPQAFD
HHHHCCCCCCHHHHH		70.7021906983
107MethylationDAFCEALRETKQGHL
HHHHHHHHHHHCCHH		57.49-
139PhosphorylationLSCDYDLSLPFPVCE
CCCCCCCCCCCCCCC		30.9722817900
151PhosphorylationVCESCPLYKKLRLST
CCCCCCCHHHHCCCC		7.39-
153UbiquitinationESCPLYKKLRLSTDT
CCCCCHHHHCCCCCC		25.86-
157PhosphorylationLYKKLRLSTDTVEHS
CHHHHCCCCCCCCHH		20.1523401153
158PhosphorylationYKKLRLSTDTVEHSL
HHHHCCCCCCCCHHC		40.0422617229
160PhosphorylationKLRLSTDTVEHSLDN
HHCCCCCCCCHHCCC		28.0728102081
164PhosphorylationSTDTVEHSLDNKDGP
CCCCCCHHCCCCCCC		24.7428450419
168UbiquitinationVEHSLDNKDGPVCLQ
CCHHCCCCCCCEEEE		64.82-
177UbiquitinationGPVCLQVKPCTPEFY
CCEEEEEECCCHHHH		22.78-
214UbiquitinationNVHFTGEKELEFRSG
CCEECCCEEEEECCC		69.78-
254UbiquitinationTAQEMQEKLQNFAQL
HHHHHHHHHHHHHHC		38.18-
284PhosphorylationHGVEGAIYGVDGKLL
CCCCCEEECCCCCCH		15.5729496907
311UbiquitinationNCPSLQNKPKMFFIQ
CCHHHCCCCCEEEEE		32.81-
335UbiquitinationGVDQQDGKNHAGSPG
CCCCCCCCCCCCCCC		54.58-
340PhosphorylationDGKNHAGSPGCEESD
CCCCCCCCCCCCCCH		20.9223401153
346PhosphorylationGSPGCEESDAGKEKL
CCCCCCCCHHCCCCC		15.5129396449
350UbiquitinationCEESDAGKEKLPKMR
CCCCHHCCCCCCCCC		54.09-
352UbiquitinationESDAGKEKLPKMRLP
CCHHCCCCCCCCCCC		73.84-
368PhosphorylationRSDMICGYACLKGTA
CCCCCHHHHHHHCCH		6.96-
374PhosphorylationGYACLKGTAAMRNTK
HHHHHHCCHHHCCCC		15.06-
384PhosphorylationMRNTKRGSWYIEALA
HCCCCCCCHHHHHHH		22.2724144214
395PhosphorylationEALAQVFSERACDMH
HHHHHHHHHHCCHHH		27.5824144214
409UbiquitinationHVADMLVKVNALIKD
HHHHHHHHHHHHHCC		26.30-
415UbiquitinationVKVNALIKDREGYAP
HHHHHHHCCCCCCCC		52.132190698
415 (in isoform 1)Ubiquitination-52.1321906983
420PhosphorylationLIKDREGYAPGTEFH
HHCCCCCCCCCCCCH		12.60-
430UbiquitinationGTEFHRCKEMSEYCS
CCCCHHHHHHHHHHH		57.31-
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
139SPhosphorylationKinasePRKDCP78527
GPS
157SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CASP2_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 CASP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRADD_HUMANCRADDphysical
15073321
PIDD1_HUMANPIDD1physical
15073321
CRADD_HUMANCRADDphysical
11156409
BID_HUMANBIDphysical
11399776
CASP2_HUMANCASP2physical
11832478
BID_HUMANBIDphysical
11832478
BCL2_HUMANBCL2genetic
11832478
B2CL1_HUMANBCL2L1genetic
11832478
CASP9_HUMANCASP9genetic
11832478
XIAP_HUMANXIAPgenetic
11832478
NOL3_HUMANNOL3physical
9560245
CCND3_HUMANCCND3physical
12011445
MDM2_HUMANMDM2physical
21726810
RAI1_HUMANRAI1physical
21900206
EF1A1_HUMANEEF1A1physical
21900206
RXRA_HUMANRXRAphysical
21900206
RL30_HUMANRPL30physical
21988832
CRADD_HUMANCRADDphysical
23049853
CRYAB_HUMANCRYABphysical
23049853
CASP2_HUMANCASP2physical
25416956
CRADD_HUMANCRADDphysical
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 CASP2_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.

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