CASPA_HUMAN - dbPTM
CASPA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CASPA_HUMAN
UniProt AC Q92851
Protein Name Caspase-10
Gene Name CASP10
Organism Homo sapiens (Human).
Sequence Length 521
Subcellular Localization
Protein Description Involved in the activation cascade of caspases responsible for apoptosis execution. Recruited to both Fas- and TNFR-1 receptors in a FADD dependent manner. May participate in the granzyme B apoptotic pathways. Cleaves and activates caspase-3, -4, -6, -7, -8, and -9. Hydrolyzes the small- molecule substrates, Tyr-Val-Ala-Asp-|-AMC and Asp-Glu-Val-Asp-|-AMC.; Isoform 7 can enhance NF-kappaB activity but promotes only slight apoptosis.; Isoform C is proteolytically inactive..
Protein Sequence MKSQGQHWYSSSDKNCKVSFREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNCTKEEVERLLPTRQRVSLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTEMTSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEKYKREKAIQIVTPPVDKEAESYQGEEELVSQTDVKTFLEALPQESWQNKHAGSNGNRATNGAPSLVSRGMQGASANTLNSETSTKRAAVYRMNRNHRGLCVIVNNHSFTSLKDRQGTHKDAEILSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCNPAHADGDCFVFCILTHGRFGAVYSSDEALIPIREIMSHFTALQCPRLAEKPKLFFIQACQGEEIQPSVSIEADALNPEQAPTSLQDSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSLCNHLKKLVPRMLKFLEKTMEIRGRKRTVWGAKQISATSLPTAISAQTPRPPMRRWSSVS
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
2Methylation------MKSQGQHWY
------CCCCCCCCC		52.03-
2Acetylation------MKSQGQHWY
------CCCCCCCCC		52.0325953088
2 (in isoform 4)Ubiquitination-52.03-
2Ubiquitination------MKSQGQHWY
------CCCCCCCCC		52.03-
3Phosphorylation-----MKSQGQHWYS
-----CCCCCCCCCC		37.9427251275
9PhosphorylationKSQGQHWYSSSDKNC
CCCCCCCCCCCCCCC		9.1328796482
10PhosphorylationSQGQHWYSSSDKNCK
CCCCCCCCCCCCCCE		20.4128796482
11PhosphorylationQGQHWYSSSDKNCKV
CCCCCCCCCCCCCEE		27.1928796482
12PhosphorylationGQHWYSSSDKNCKVS
CCCCCCCCCCCCEEE		46.8128796482
14UbiquitinationHWYSSSDKNCKVSFR
CCCCCCCCCCEEEEC		67.22-
17UbiquitinationSSSDKNCKVSFREKL
CCCCCCCEEEECCCE		50.75-
23UbiquitinationCKVSFREKLLIIDSN
CEEEECCCEEEEECC		44.32-
90UbiquitinationLYIIRQKKLLQHLNC
HHHHHHHHHHHHCCC		46.20-
99UbiquitinationLQHLNCTKEEVERLL
HHHCCCCHHHHHHHC		54.82-
99 (in isoform 4)Ubiquitination-54.82-
158UbiquitinationSFLAFLEKQGKIDED
HHHHHHHHCCCCCCC		67.51-
161 (in isoform 4)Ubiquitination-44.48-
161UbiquitinationAFLEKQGKIDEDNLT
HHHHHCCCCCCCCCH		44.48-
161UbiquitinationAFLEKQGKIDEDNLT
HHHHHCCCCCCCCCH		44.48-
175UbiquitinationTCLEDLCKTVVPKLL
HHHHHHHHHHHHHHH		52.21-
176PhosphorylationCLEDLCKTVVPKLLR
HHHHHHHHHHHHHHH		26.2424719451
180UbiquitinationLCKTVVPKLLRNIEK
HHHHHHHHHHHHHHH		48.85-
180 (in isoform 4)Ubiquitination-48.85-
180UbiquitinationLCKTVVPKLLRNIEK
HHHHHHHHHHHHHHH		48.85-
192UbiquitinationIEKYKREKAIQIVTP
HHHHCHHHCEEEECC		55.62-
192UbiquitinationIEKYKREKAIQIVTP
HHHHCHHHCEEEECC		55.62-
192 (in isoform 4)Ubiquitination-55.62-
198PhosphorylationEKAIQIVTPPVDKEA
HHCEEEECCCCCHHH		24.4122985185
207PhosphorylationPVDKEAESYQGEEEL
CCCHHHHHCCCHHHH		29.7827251275
216PhosphorylationQGEEELVSQTDVKTF
CCHHHHHCHHHHHHH		39.7317525332
235UbiquitinationPQESWQNKHAGSNGN
CHHHHHCCCCCCCCC		21.52-
250PhosphorylationRATNGAPSLVSRGMQ
CCCCCCCCHHHHCCC		40.6528111955
253PhosphorylationNGAPSLVSRGMQGAS
CCCCCHHHHCCCCCC		28.5428111955
260PhosphorylationSRGMQGASANTLNSE
HHCCCCCCCCCCCCC		28.9527251275
263PhosphorylationMQGASANTLNSETST
CCCCCCCCCCCCHHH		27.3423312004
266PhosphorylationASANTLNSETSTKRA
CCCCCCCCCHHHHHH		45.4223401153
268PhosphorylationANTLNSETSTKRAAV
CCCCCCCHHHHHHHH		41.3328857561
269PhosphorylationNTLNSETSTKRAAVY
CCCCCCHHHHHHHHH		28.0728857561
270PhosphorylationTLNSETSTKRAAVYR
CCCCCHHHHHHHHHH		31.7828857561
271 (in isoform 4)Ubiquitination-39.55-
271UbiquitinationLNSETSTKRAAVYRM
CCCCHHHHHHHHHHC		39.55-
276PhosphorylationSTKRAAVYRMNRNHR
HHHHHHHHHCCCCCC		10.2224719451
293PhosphorylationCVIVNNHSFTSLKDR
EEEECCCCCCCCCCC		32.1327251275
338UbiquitinationEMEMVLQKQKCNPAH
EHHHHHHHCCCCHHH		47.79-
411 (in isoform 6)Phosphorylation-21.0322210691
435 (in isoform 2)Phosphorylation-26.6522210691
454 (in isoform 6)Phosphorylation-58.3923285258
455 (in isoform 2)Ubiquitination-15.24-
466 (in isoform 2)Ubiquitination-3.05-
467 (in isoform 2)Ubiquitination-36.19-
478 (in isoform 2)Phosphorylation-50.0023285258
478 (in isoform 4)Phosphorylation-50.0022210691
489PhosphorylationEIRGRKRTVWGAKQI
HHCCCCCCCCCCEEE		24.5222210691
498 (in isoform 4)Ubiquitination-11.66-
499PhosphorylationGAKQISATSLPTAIS
CCEEEECCCCCCCHH		24.8123612710
500PhosphorylationAKQISATSLPTAISA
CEEEECCCCCCCHHC		31.8728851738
503PhosphorylationISATSLPTAISAQTP
EECCCCCCCHHCCCC		41.7528851738
506PhosphorylationTSLPTAISAQTPRPP
CCCCCCHHCCCCCCC		16.3223612710
509 (in isoform 4)Ubiquitination-22.45-
509PhosphorylationPTAISAQTPRPPMRR
CCCHHCCCCCCCCCC		22.4528851738
510 (in isoform 4)Ubiquitination-34.40-
521PhosphorylationMRRWSSVS-------
CCCCCCCC-------		36.1327251275
521 (in isoform 4)Phosphorylation-36.1323285258
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
-KUbiquitinationE3 ubiquitin ligaseRNF34Q969K3
PMID:15069192
-KUbiquitinationE3 ubiquitin ligaseRFFLQ8WZ73
PMID:15069192
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CASPA_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 CASPA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TR10B_HUMANTNFRSF10Bphysical
15659383
FADD_HUMANFADDphysical
15659383
TNFL6_HUMANFASLGphysical
15659383
CASP8_HUMANCASP8physical
15659383
TNR1A_HUMANTNFRSF1Aphysical
15659383
CFLAR_HUMANCFLARphysical
12887920
CASP8_HUMANCASP8physical
12887920
FADD_HUMANFADDphysical
9228018
CFLAR_HUMANCFLARphysical
9228018
TRAF1_HUMANTRAF1physical
11098060
RYBP_HUMANRYBPphysical
11395500
FADD_HUMANFADDphysical
11717445
RIPK1_HUMANRIPK1physical
11002417
M3K14_HUMANMAP3K14physical
11002417
CASP2_HUMANCASP2physical
8962078
CASP4_HUMANCASP4physical
8962078
CASP3_HUMANCASP3physical
8962078
CASP7_HUMANCASP7physical
8962078
CASPA_HUMANCASP10physical
8962078
CASP8_HUMANCASP8physical
8962078
CASP9_HUMANCASP9physical
8962078
CASP6_HUMANCASP6physical
8962078
CASP1_HUMANCASP1physical
8962078
DEDD2_HUMANDEDD2physical
12527898
DEDD_HUMANDEDDphysical
12527898
GPA1_YEASTGPA1genetic
22782902
PP2A1_YEASTPPH21genetic
22782902
KAPA_YEASTTPK1genetic
22782902
FAR3_YEASTFAR3genetic
22782902
ATG1_YEASTATG1genetic
22782902
MSN2_YEASTMSN2genetic
22782902
GAL4_YEASTGAL4genetic
22782902
RL21B_YEASTRPL21Bgenetic
22782902
STE7_YEASTSTE7genetic
22782902
PP2A2_YEASTPPH22genetic
22782902
KAPB_YEASTTPK2genetic
22782902
FAR7_YEASTFAR7genetic
22782902
ATG4_YEASTATG4genetic
22782902
GLN3_YEASTGLN3genetic
22782902
SSN2_YEASTSSN2genetic
22782902
MDM30_YEASTMDM30genetic
22782902
STE11_YEASTSTE11genetic
22782902
PP4C_YEASTPPH3genetic
22782902
KAPC_YEASTTPK3genetic
22782902
FAR8_YEASTFAR8genetic
22782902
BECN1_YEASTVPS30genetic
22782902
ASG1_YEASTASG1genetic
22782902
PMT5_YEASTPMT5genetic
22782902
BFR1_YEASTBFR1genetic
22782902
STE20_YEASTSTE20genetic
22782902
PP2C2_YEASTPTC2genetic
22782902
VPS64_YEASTVPS64genetic
22782902
ATG8_YEASTATG8genetic
22782902
TREA_YEASTNTH1genetic
22782902
MPH1_YEASTMPH1genetic
22782902
ORT1_YEASTORT1genetic
22782902
FUS3_YEASTFUS3genetic
22782902
PP2C3_YEASTPTC3genetic
22782902
FAR10_YEASTFAR10genetic
22782902
ATG13_YEASTATG13genetic
22782902
MBR1_YEASTMBR1genetic
22782902
DOA10_YEASTSSM4genetic
22782902
CWP1_YEASTCWP1genetic
22782902
KSS1_YEASTKSS1genetic
22782902
FAR11_YEASTFAR11genetic
22782902
ITT1_YEASTITT1genetic
22782902
AIM9_YEASTAIM9genetic
22782902
SLT2_YEASTSLT2genetic
22782902
LDB18_YEASTLDB18genetic
22782902
CUP9_YEASTCUP9genetic
22782902
WHI3_YEASTWHI3genetic
22782902
C8AP2_HUMANCASP8AP2physical
15069192
FADD_HUMANFADDphysical
15069192
RNF34_HUMANRNF34physical
15069192
RB_HUMANRB1physical
15735701
RIOK3_HUMANRIOK3physical
21988832
IKBL1_HUMANNFKBIL1physical
21988832
P20L1_HUMANPHF20L1physical
21988832
MS18B_HUMANOIP5physical
21988832
PRDX6_HUMANPRDX6physical
20829884
FADD_HUMANFADDphysical
20829884
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603909Autoimmune lymphoproliferative syndrome 2A (ALPS2A)
605027Familial non-Hodgkin lymphoma (NHL)
613659Gastric cancer (GASC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CASPA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.

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