CBY1_HUMAN - dbPTM
CBY1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CBY1_HUMAN
UniProt AC Q9Y3M2
Protein Name Protein chibby homolog 1
Gene Name CBY1
Organism Homo sapiens (Human).
Sequence Length 126
Subcellular Localization Nucleus speckle . Cytoplasm, cytoskeleton, cilium basal body . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Golgi apparatus. Golgi apparatus, trans-Golgi network .
Protein Description Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellular proteins. Promotes adipocyte and cardiomyocyte differentiation..
Protein Sequence MPFFGNTFSPKKTPPRKSASLSNLHSLDRSTREVELGLEYGSPTMNLAGQSLKFENGQWIAETGVSGGVDRREVQRLRRRNQQLEEENNLLRLKVDILLDMLSESTAESHLMEKELDELRISRKRK
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
7Phosphorylation-MPFFGNTFSPKKTP
-CCCCCCCCCCCCCC
26.3529255136
9PhosphorylationPFFGNTFSPKKTPPR
CCCCCCCCCCCCCCC
33.5029255136
13PhosphorylationNTFSPKKTPPRKSAS
CCCCCCCCCCCCCCC
44.6528555341
18PhosphorylationKKTPPRKSASLSNLH
CCCCCCCCCCCCCHH
25.1130266825
20PhosphorylationTPPRKSASLSNLHSL
CCCCCCCCCCCHHHC
39.1530266825
22PhosphorylationPRKSASLSNLHSLDR
CCCCCCCCCHHHCCC
34.5530266825
26PhosphorylationASLSNLHSLDRSTRE
CCCCCHHHCCCCCCE
34.8223927012
30PhosphorylationNLHSLDRSTREVELG
CHHHCCCCCCEEHHH
31.3322210691
31PhosphorylationLHSLDRSTREVELGL
HHHCCCCCCEEHHHH
31.5722210691
42PhosphorylationELGLEYGSPTMNLAG
HHHHHCCCCCCCCCC
19.1228348404
44PhosphorylationGLEYGSPTMNLAGQS
HHHCCCCCCCCCCCE
22.0128348404
51PhosphorylationTMNLAGQSLKFENGQ
CCCCCCCEEEEECCE
32.3922210691
52PhosphorylationMNLAGQSLKFENGQW
CCCCCCEEEEECCEE
5.9119413330
61PhosphorylationFENGQWIAETGVSGG
EECCEEEHHHCCCCC
12.82-
63PhosphorylationNGQWIAETGVSGGVD
CCEEEHHHCCCCCCC
33.5822210691
66PhosphorylationWIAETGVSGGVDRRE
EEHHHCCCCCCCHHH
31.0428555341
69PhosphorylationETGVSGGVDRREVQR
HHCCCCCCCHHHHHH
6.2027251275

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
20SPhosphorylationKinaseAKT1P31749
PSP
20SPhosphorylationKinaseAKT2P31751
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CBY1_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 CBY1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
12712206
NBPFB_HUMANNBPF11physical
20096688
CTNB1_HUMANCTNNB1physical
20096688
CLUS_HUMANCLUphysical
20096688
FA92A_HUMANFAM92A1physical
25416956
TT23L_HUMANTTC23Lphysical
25416956
CFA53_HUMANCFAP53physical
25416956
MAP7_HUMANMAP7physical
27173435
MARK2_HUMANMARK2physical
27173435
CE170_HUMANCEP170physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
CING_HUMANCGNphysical
27173435
GGYF1_HUMANGIGYF1physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
GGYF2_HUMANGIGYF2physical
27173435
HDAC4_HUMANHDAC4physical
27173435
NGAP_HUMANRASAL2physical
27173435
SYDE1_HUMANSYDE1physical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
F110B_HUMANFAM110Bphysical
27173435
NAV1_HUMANNAV1physical
27173435
HDAC7_HUMANHDAC7physical
27173435
F110A_HUMANFAM110Aphysical
27173435
RPTOR_HUMANRPTORphysical
27173435
KIF1B_HUMANKIF1Bphysical
27173435
REEP3_HUMANREEP3physical
27173435
CRTC2_HUMANCRTC2physical
27173435
CRTC3_HUMANCRTC3physical
27173435
SH3B4_HUMANSH3BP4physical
27173435
CRTC1_HUMANCRTC1physical
27173435
CLAP1_HUMANCLASP1physical
27173435
REEP4_HUMANREEP4physical
27173435
DAB2P_HUMANDAB2IPphysical
27173435
ARAF_HUMANARAFphysical
27173435
UBP8_HUMANUSP8physical
27173435
MFR1L_HUMANMTFR1Lphysical
27173435
DCP1A_HUMANDCP1Aphysical
27173435
HDAC5_HUMANHDAC5physical
27173435
SPIR1_HUMANSPIRE1physical
27173435
PRPS2_HUMANPRPS2physical
27173435
PI4KB_HUMANPI4KBphysical
27173435
BAD_HUMANBADphysical
27173435
DCP1B_HUMANDCP1Bphysical
27173435

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 CBY1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-9, AND MASSSPECTROMETRY.

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