CASP4_HUMAN - dbPTM
CASP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CASP4_HUMAN
UniProt AC P49662
Protein Name Caspase-4
Gene Name CASP4
Organism Homo sapiens (Human).
Sequence Length 377
Subcellular Localization Cytoplasm, cytosol . Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side . Mitochondrion . Inflammasome . Secreted . Predominantly localizes to the endoplasmic reticulum (ER). Association with the ER membrane requires TMEM
Protein Description Inflammatory caspase. [PubMed: 7797510]
Protein Sequence MAEGNHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQISPNKKAHPNMEAGPPESGESTDALKLCPHEEFLRLCKERAEEIYPIKERNNRTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFLVLMSHGILEGICGTVHDEKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGANRGELWVRDSPASLEVASSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPRAKAQMPTIERLSMTRYFYLFPGN
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
2 (in isoform 2)Acetylation-33.1422814378
16PhosphorylationKPLKVLESLGKDFLT
CCHHHHHHHCCHHHH		37.9628355574
31UbiquitinationGVLDNLVEQNVLNWK
HHHHHHHHHCCCCCC		39.3429967540
38UbiquitinationEQNVLNWKEEEKKKY
HHCCCCCCHHHHHHH		54.9227667366
49MethylationKKKYYDAKTEDKVRV
HHHHCCCCCHHHHHH		49.9323644510
51UbiquitinationKYYDAKTEDKVRVMA
HHCCCCCHHHHHHHH		55.9429967540
53MethylationYDAKTEDKVRVMADS
CCCCCHHHHHHHHHH		26.2123644510
73UbiquitinationRMAGQMLLQTFFNID
HHHHHHHHHHHHCHH		3.6527667366
75PhosphorylationAGQMLLQTFFNIDQI
HHHHHHHHHHCHHHC		30.1128176443
83 (in isoform 3)Phosphorylation-19.4520068231
83PhosphorylationFFNIDQISPNKKAHP
HHCHHHCCCCCCCCC		19.4529255136
87UbiquitinationDQISPNKKAHPNMEA
HHCCCCCCCCCCCCC		59.5829967540
92SulfoxidationNKKAHPNMEAGPPES
CCCCCCCCCCCCCCC		4.3830846556
107UbiquitinationGESTDALKLCPHEEF
CCCCCHHHHCCHHHH		50.1729967540
129UbiquitinationAEEIYPIKERNNRTR
HHHHCCCCCCCCCCE		46.2327667366
225UbiquitinationGTVHDEKKPDVLLYD
CCCCCCCCCCEEEEH		44.39-
233PhosphorylationPDVLLYDTIFQIFNN
CCEEEEHHHHHHHCC		15.3325690035
254UbiquitinationKDKPKVIIVQACRGA
CCCCEEEEEEECCCC		1.7927667366
271PhosphorylationGELWVRDSPASLEVA
CCCEEECCCHHEEEC		16.2925159151
274PhosphorylationWVRDSPASLEVASSQ
EEECCCHHEEECCCC		28.5721712546
279PhosphorylationPASLEVASSQSSENL
CHHEEECCCCCCCCH		33.8027732954
280PhosphorylationASLEVASSQSSENLE
HHEEECCCCCCCCHH		25.0926657352
282PhosphorylationLEVASSQSSENLEED
EEECCCCCCCCHHCC		41.3829978859
283PhosphorylationEVASSQSSENLEEDA
EECCCCCCCCHHCCC		23.9027732954
289UbiquitinationSSENLEEDAVYKTHV
CCCCHHCCCHHHHHH		31.7727667366
292PhosphorylationNLEEDAVYKTHVEKD
CHHCCCHHHHHHCCC		16.3427732954
294PhosphorylationEEDAVYKTHVEKDFI
HCCCHHHHHHCCCCE		17.2929978859
345UbiquitinationHLEEVFRKVQQSFET
CHHHHHHHHHHHCCC		32.6927667366
345MalonylationHLEEVFRKVQQSFET
CHHHHHHHHHHHCCC		32.6926320211
352PhosphorylationKVQQSFETPRAKAQM
HHHHHCCCHHHHCCC		18.9625159151
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 CASP4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CASP4_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 CASP4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMC3_HUMANSMC3physical
17353931
C1TM_HUMANMTHFD1Lphysical
17353931
GELS_HUMANGSNphysical
17353931
DAAF5_HUMANDNAAF5physical
17353931
SRPRB_HUMANSRPRBphysical
17353931
NUP93_HUMANNUP93physical
17353931
MYBPP_HUMANMYCBPAPphysical
17353931
GHC1_HUMANSLC25A22physical
17353931
SMC1A_HUMANSMC1Aphysical
17353931
CDK2_HUMANCDK2physical
17353931
PSB1_HUMANPSMB1physical
17353931
SMC2_HUMANSMC2physical
17353931
MSH6_HUMANMSH6physical
17353931
IF2G_HUMANEIF2S3physical
17353931
CNBP1_HUMANCTNNBIP1physical
17353931
GCN1_HUMANGCN1L1physical
17353931
USP9X_HUMANUSP9Xphysical
17353931
UFL1_HUMANUFL1physical
17353931
VDAC3_HUMANVDAC3physical
17353931
IL37_HUMANIL37physical
12096920
IL18_HUMANIL18physical
12096920
A4_HUMANAPPphysical
21832049
ELF4_HUMANELF4physical
21988832
MYH9_HUMANMYH9physical
21988832
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 CASP4_HUMAN

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Related Literatures of Post-Translational Modification
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-83, AND MASSSPECTROMETRY.

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