TTC33_HUMAN - dbPTM
TTC33_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTC33_HUMAN
UniProt AC Q6PID6
Protein Name Tetratricopeptide repeat protein 33
Gene Name TTC33
Organism Homo sapiens (Human).
Sequence Length 262
Subcellular Localization
Protein Description
Protein Sequence MASFGWKRKIGEKVSKVTSQQFEAEAADEKDVVDNDEGNWLHAIKRRKEILLEGCAEKSKQLKDEGASLAENKRYREAIQKWDEALQLTPNDATLYEMKSQVLMSLHEMFPAVHAAEMAVQQNPHSWESWQTLGRAQLGLGEIILAIRSFQVALHIYPMNPEIWKEDLSWARTLQEQQKVAQRIKKSEAPAEVTHFSPKSIPDYDFESDEIVAVCAAIAEKEKTVSANKTMVIVSASGAIETVTEKEDGATPPDGSVFIKAR
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
7Acetylation-MASFGWKRKIGEKV
-CCCCCCHHHHHHHH		44.1625953088
13UbiquitinationWKRKIGEKVSKVTSQ
CHHHHHHHHHHHHHH		46.7422817900
13AcetylationWKRKIGEKVSKVTSQ
CHHHHHHHHHHHHHH		46.7423749302
16UbiquitinationKIGEKVSKVTSQQFE
HHHHHHHHHHHHHHH		53.1421906983
30UbiquitinationEAEAADEKDVVDNDE
HHHHCCCCCCCCCCC		57.2729967540
45AcetylationGNWLHAIKRRKEILL
CCHHHHHHHHHHHHH		47.1125953088
45UbiquitinationGNWLHAIKRRKEILL
CCHHHHHHHHHHHHH		47.1132015554
48UbiquitinationLHAIKRRKEILLEGC
HHHHHHHHHHHHHHH		53.8129967540
58AcetylationLLEGCAEKSKQLKDE
HHHHHHHHHHHHHHH		44.4125953088
58UbiquitinationLLEGCAEKSKQLKDE
HHHHHHHHHHHHHHH		44.4129967540
60UbiquitinationEGCAEKSKQLKDEGA
HHHHHHHHHHHHHCC		71.38-
63SumoylationAEKSKQLKDEGASLA
HHHHHHHHHHCCHHH		51.76-
63SumoylationAEKSKQLKDEGASLA
HHHHHHHHHHCCHHH		51.76-
73UbiquitinationGASLAENKRYREAIQ
CCHHHHHHHHHHHHH		42.1629967540
94PhosphorylationQLTPNDATLYEMKSQ
CCCCCCCHHHHHHHH		32.5120068231
157PhosphorylationFQVALHIYPMNPEIW
HHHHHEECCCCHHHH		5.9120068231
179UbiquitinationRTLQEQQKVAQRIKK
HHHHHHHHHHHHHHH		38.9521906983
186UbiquitinationKVAQRIKKSEAPAEV
HHHHHHHHCCCCCCC		51.6729967540
186SumoylationKVAQRIKKSEAPAEV
HHHHHHHHCCCCCCC		51.67-
186SumoylationKVAQRIKKSEAPAEV
HHHHHHHHCCCCCCC		51.67-
187PhosphorylationVAQRIKKSEAPAEVT
HHHHHHHCCCCCCCC		33.7123927012
194PhosphorylationSEAPAEVTHFSPKSI
CCCCCCCCCCCCCCC		14.5423927012
197PhosphorylationPAEVTHFSPKSIPDY
CCCCCCCCCCCCCCC		24.6629255136
200PhosphorylationVTHFSPKSIPDYDFE
CCCCCCCCCCCCCCC		42.6226074081
204PhosphorylationSPKSIPDYDFESDEI
CCCCCCCCCCCHHHH		19.7126074081
208PhosphorylationIPDYDFESDEIVAVC
CCCCCCCHHHHHHHH		40.3027732954
226PhosphorylationAEKEKTVSANKTMVI
HHHHCCCCCCCEEEE		31.2129396449
235PhosphorylationNKTMVIVSASGAIET
CCEEEEEECCCCEEE		12.9528122231
237PhosphorylationTMVIVSASGAIETVT
EEEEEECCCCEEECE		22.6628122231
242PhosphorylationSASGAIETVTEKEDG
ECCCCEEECEECCCC		26.9828122231
244PhosphorylationSGAIETVTEKEDGAT
CCCEEECEECCCCCC		49.0828122231
246UbiquitinationAIETVTEKEDGATPP
CEEECEECCCCCCCC		52.30-
251PhosphorylationTEKEDGATPPDGSVF
EECCCCCCCCCCCCE		40.6625159151
256PhosphorylationGATPPDGSVFIKAR-
CCCCCCCCCEEEEC-		22.6429396449
260SumoylationPDGSVFIKAR-----
CCCCCEEEEC-----		27.00-
260UbiquitinationPDGSVFIKAR-----
CCCCCEEEEC-----		27.0029967540
260SumoylationPDGSVFIKAR-----
CCCCCEEEEC-----		27.00-
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 TTC33_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTC33_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 TTC33_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
23455924
SMYD1_HUMANSMYD1physical
23455924
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 TTC33_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-197, 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-197, 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-197, AND MASSSPECTROMETRY.
"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-251, AND MASSSPECTROMETRY.

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