CAAP1_HUMAN - dbPTM
CAAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAAP1_HUMAN
UniProt AC Q9H8G2
Protein Name Caspase activity and apoptosis inhibitor 1
Gene Name CAAP1
Organism Homo sapiens (Human).
Sequence Length 361
Subcellular Localization
Protein Description Anti-apoptotic protein that modulates a caspase-10 dependent mitochondrial caspase-3/9 feedback amplification loop..
Protein Sequence MTGKKSSREKRRKRSSQEAAAALAAPDIVPALASGSSGSTSGCGSAGGCGSVSCCGNANFSGSVTGGGSGGSCWGGSSVERSERRKRRSTDSSSVSGSLQQETKYILPTLEKELFLAEHSDLEEGGLDLTVSLKPVSFYISDKKEMLQQCFCIIGEKKLQKMLPDVLKNCSIEEIKKLCQEQLELLSEKKILKILEGDNGMDSDMEEEADDGSKMGSDLVSQQDICIDSASSVRENKQPEGLELKQGKGEDSDVLSINADAYDSDIEGPCNEEAAAPEAPENTVQSEAGQIDDLEKDIEKSVNEILGLAESSPNEPKAATLAVPPPEDVQPSAQQLELLELEMRARAIKALMKAGDIKKPA
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
6Phosphorylation--MTGKKSSREKRRK
--CCCCHHHHHHHHH		37.8120068231
7Phosphorylation-MTGKKSSREKRRKR
-CCCCHHHHHHHHHH		54.0320068231
44UbiquitinationSGSTSGCGSAGGCGS
CCCCCCCCCCCCCCC		24.8532015554
58PhosphorylationSVSCCGNANFSGSVT
CEECCCCCCCCCCCC		12.0632142685
89PhosphorylationSERRKRRSTDSSSVS
HHHHHHCCCCCCCCC		40.3723927012
90PhosphorylationERRKRRSTDSSSVSG
HHHHHCCCCCCCCCH		37.7822167270
92PhosphorylationRKRRSTDSSSVSGSL
HHHCCCCCCCCCHHH		25.3022167270
93PhosphorylationKRRSTDSSSVSGSLQ
HHCCCCCCCCCHHHH		37.2522167270
94PhosphorylationRRSTDSSSVSGSLQQ
HCCCCCCCCCHHHHH		25.0125159151
96PhosphorylationSTDSSSVSGSLQQET
CCCCCCCCHHHHHHH		25.3123927012
98PhosphorylationDSSSVSGSLQQETKY
CCCCCCHHHHHHHEE		18.5923927012
103PhosphorylationSGSLQQETKYILPTL
CHHHHHHHEEEHHHH		25.4723403867
104SumoylationGSLQQETKYILPTLE
HHHHHHHEEEHHHHH		29.5528112733
105PhosphorylationSLQQETKYILPTLEK
HHHHHHEEEHHHHHH		18.3427642862
109PhosphorylationETKYILPTLEKELFL
HHEEEHHHHHHHHHH		44.0724173317
120PhosphorylationELFLAEHSDLEEGGL
HHHHEECCCCCCCCC		35.0827422710
155UbiquitinationQQCFCIIGEKKLQKM
HHHHHHHCHHHHHHH		22.2829967540
167PhosphorylationQKMLPDVLKNCSIEE
HHHCHHHHHCCCHHH		4.2632142685
176AcetylationNCSIEEIKKLCQEQL
CCCHHHHHHHHHHHH		42.8627452117
187PhosphorylationQEQLELLSEKKILKI
HHHHHHHCCHHHHHH		61.0523663014
1892-HydroxyisobutyrylationQLELLSEKKILKILE
HHHHHCCHHHHHHHH		41.56-
189AcetylationQLELLSEKKILKILE
HHHHHCCHHHHHHHH		41.5626051181
189UbiquitinationQLELLSEKKILKILE
HHHHHCCHHHHHHHH		41.5632015554
190UbiquitinationLELLSEKKILKILEG
HHHHCCHHHHHHHHC		49.58-
203PhosphorylationEGDNGMDSDMEEEAD
HCCCCCCCCCHHHCC		29.9322167270
213PhosphorylationEEEADDGSKMGSDLV
HHHCCCCCCCCHHHH		26.8520363803
217PhosphorylationDDGSKMGSDLVSQQD
CCCCCCCHHHHHHCC		25.0322777824
221PhosphorylationKMGSDLVSQQDICID
CCCHHHHHHCCEEEE		29.4417525332
229PhosphorylationQQDICIDSASSVREN
HCCEEEECHHHHHHC		15.3327251275
231PhosphorylationDICIDSASSVRENKQ
CEEEECHHHHHHCCC		33.0627251275
232PhosphorylationICIDSASSVRENKQP
EEEECHHHHHHCCCC		25.5527251275
256PhosphorylationGEDSDVLSINADAYD
CCCCCCEEEECCCCC		17.4129802988
262PhosphorylationLSINADAYDSDIEGP
EEEECCCCCCCCCCC		19.2728348404
264PhosphorylationINADAYDSDIEGPCN
EECCCCCCCCCCCCC		28.0130257219
300UbiquitinationDLEKDIEKSVNEILG
HHHHHHHHHHHHHHH		61.1029967540
301PhosphorylationLEKDIEKSVNEILGL
HHHHHHHHHHHHHHH		19.8625159151
311PhosphorylationEILGLAESSPNEPKA
HHHHHHHCCCCCCCC		45.5522167270
312PhosphorylationILGLAESSPNEPKAA
HHHHHHCCCCCCCCE		24.2119664994
349AcetylationEMRARAIKALMKAGD
HHHHHHHHHHHHHCC		34.1912436885
349UbiquitinationEMRARAIKALMKAGD
HHHHHHHHHHHHHCC		34.19-
353AcetylationRAIKALMKAGDIKKP
HHHHHHHHHCCCCCC		50.4912436895
359AcetylationMKAGDIKKPA-----
HHHCCCCCCC-----		46.6512436905
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
203SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAAP1_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 CAAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC4_HUMANXRCC4physical
16169070
KAT7_HUMANKAT7physical
16169070
PTN_HUMANPTNphysical
16169070
A4_HUMANAPPphysical
21832049
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 CAAP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-312, ANDMASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-90; SER-92; SER-94;SER-203 AND SER-312, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.
"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-203 AND SER-312, ANDMASS SPECTROMETRY.
"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-221, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.

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