CU059_HUMAN - dbPTM
CU059_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CU059_HUMAN
UniProt AC P57076
Protein Name UPF0769 protein C21orf59
Gene Name C21orf59
Organism Homo sapiens (Human).
Sequence Length 290
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, cilium basal body . Partially colocalized with SASS6 in cytoplasmic puncta, suggesting a centrosomal localization.
Protein Description Plays a role in motile cilium function, possibly by acting on outer dynein arm assembly. [PubMed: 24094744 Seems to be important for initiation rather than maintenance of cilium motility (By similarity Required for correct positioning of the cilium at the apical cell surface, suggesting an additional role in the planar cell polarity (PCP) pathway (By similarity May suppress canonical Wnt signaling activity (By similarity]
Protein Sequence MVLLHVKRGDESQFLLQAPGSTELEELTVQVARVYNGRLKVQRLCSEMEELAEHGIFLPPNMQGLTDDQIEELKLKDEWGEKCVPSGGAVFKKDDIGRRNGQAPNEKMKQVLKKTIEEAKAIISKKQVEAGVCVTMEMVKDALDQLRGAVMIVYPMGLPPYDPIRMEFENKEDLSGTQAGLNVIKEAEAQLWWAAKELRRTKKLSDYVGKNEKTKIIAKIQQRGQGAPAREPIISSEEQKQLMLYYHRRQEELKRLEENDDDAYLNSPWADNTALKRHFHGVKDIKWRPR
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
219AcetylationEKTKIIAKIQQRGQG
CCHHHHHHHHHCCCC
30.5525953088

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 CU059_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CU059_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 CU059_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PEX7_HUMANPEX7physical
26186194
PLAK_HUMANJUPphysical
26186194
HUTH_HUMANHALphysical
26186194
CALL5_HUMANCALML5physical
26186194
TGM1_HUMANTGM1physical
26186194
APRV1_HUMANASPRV1physical
26186194
TGM3_HUMANTGM3physical
26186194
RNAS7_HUMANRNASE7physical
26186194
FILA_HUMANFLGphysical
26186194
SAP3_HUMANGM2Aphysical
26186194
POF1B_HUMANPOF1Bphysical
26186194
CDSN_HUMANCDSNphysical
26186194
SPA12_HUMANSERPINA12physical
26186194
SPB8_HUMANSERPINB8physical
26186194
CBPA4_HUMANCPA4physical
26186194
PAI2_HUMANSERPINB2physical
26186194
FBX50_HUMANNCCRP1physical
26186194
ECM1_HUMANECM1physical
26186194
GLRX1_HUMANGLRXphysical
26186194
SPB7_HUMANSERPINB7physical
26186194
KLK5_HUMANKLK5physical
26186194
HNRH1_HUMANHNRNPH1physical
26344197
PLXB1_HUMANPLXNB1physical
26496610
STK3_HUMANSTK3physical
26496610
ARK72_HUMANAKR7A2physical
26496610
SCC4_HUMANMAU2physical
26496610
PGAP2_HUMANPGAP2physical
26496610
ILKAP_HUMANILKAPphysical
26496610
CU059_HUMANC21orf59physical
26472760
CTNA1_HUMANCTNNA1physical
26472760
CTNB1_HUMANCTNNB1physical
26472760
GLRX1_HUMANGLRXphysical
28514442
PEX7_HUMANPEX7physical
28514442
SPB8_HUMANSERPINB8physical
28514442
SPB7_HUMANSERPINB7physical
28514442
PAI2_HUMANSERPINB2physical
28514442
HPBP1_HUMANHSPBP1physical
28514442
CDSN_HUMANCDSNphysical
28514442
ECM1_HUMANECM1physical
28514442
CBPA4_HUMANCPA4physical
28514442
HUTH_HUMANHALphysical
28514442
HSP7C_HUMANHSPA8physical
28514442
RNAS7_HUMANRNASE7physical
28514442
SPA12_HUMANSERPINA12physical
28514442
FBX50_HUMANNCCRP1physical
28514442
KLK5_HUMANKLK5physical
28514442
FILA_HUMANFLGphysical
28514442
POF1B_HUMANPOF1Bphysical
28514442
TGM1_HUMANTGM1physical
28514442
ARGI1_HUMANARG1physical
28514442
DSG1_HUMANDSG1physical
28514442
SAP3_HUMANGM2Aphysical
28514442
CALL5_HUMANCALML5physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615500Ciliary dyskinesia, primary, 26 (CILD26)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CU059_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-264, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-210, AND MASSSPECTROMETRY.

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