Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Calcyclin-binding protein  

UniProtKB / Swiss-Prot ID :  CYBP_HUMAN

Gene Name (Synonyms) : 
CACYBP, S100A6BP, SIP PNAS-107  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm. Note=Cytoplasmic at low calcium concentrations. In neuroblastoma cells, after a retinoic acid (RA) induction and calcium increase, it localizes in both the nucleus and cytoplasm. The nuclear fraction may be phosphorylated. 

Protein Function :  May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1). 

Protein Sequence MASEELQKDLEEVKVLLEKATRKRVRDALTAEKSKIETEIKNKMQQKSQKKAELLDNEKPAAVVAPITTG...
Predicted Secondary Structure CCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCEECC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASEEL
---CCHHHH
26.16UniProtKB
Link-
8N6-acetyllysineEELQKDLEE
HHHHHHHHH
76.53HPRD
Link-
8N6-acetyllysineEELQKDLEE
HHHHHHHHH
76.53Phosphositeplus
Link-
8N6-acetyllysine.EELQKDLEE
HHHHHHHHH
76.53UniProtKB
Link-
14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEEVKVLLE
HHHHHHHHH
30.37Phosphositeplus
Link-
19N6-acetyllysineVLLEKATRK
HHHHHHHHH
55.84HPRD
Link-
19N6-acetyllysineVLLEKATRK
HHHHHHHHH
55.84Phosphositeplus
Link-
19N6-acetyllysine.VLLEKATRK
HHHHHHHHH
55.84UniProtKB
Link-
85Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DQSDKFVKI
CCCCCEEEE
58.25Phosphositeplus
Link
85N6-acetyllysineDQSDKFVKI
CCCCCEEEE
58.25HPRD
Link
85N6-acetyllysineDQSDKFVKI
CCCCCEEEE
58.25Phosphositeplus
Link
85N6-acetyllysine.DQSDKFVKI
CCCCCEEEE
58.25UniProtKB
Link
118N6-acetyllysineDLLVKNLNG
EEEEECCCC
56.54HPRD
Link
118N6-acetyllysineDLLVKNLNG
EEEEECCCC
56.54Phosphositeplus
Link
118N6-acetyllysine.DLLVKNLNG
EEEEECCCC
56.54UniProtKB
Link
123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NLNGKSYSM
CCCCCCCEE
45.18Phosphositeplus
Link
134N6-acetyllysineNNLLKPISV
HHHHCCCCC
43.39HPRD
Link
134N6-acetyllysineNNLLKPISV
HHHHCCCCC
43.39Phosphositeplus
Link
134N6-acetyllysine.NNLLKPISV
HHHHCCCCC
43.39UniProtKB
Link
141PhosphoserineSVEGSSKKV
CCCCCEEEE
26.02Phosphositeplus
Link
178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KEKEKPSYD
CHHHCCCCC
50.78Phosphositeplus
Link-
181PhosphotyrosineEKPSYDTET
HCCCCCCCC
35.10Phosphositeplus
Link-
196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MNVLKKIYE
HHHHHHHHC
32.61Phosphositeplus
Link-
197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NVLKKIYED
HHHHHHHCC
46.49Phosphositeplus
Link-
199PhosphotyrosineLKKIYEDGD
HHHHHCCCC
19.49HPRD
Link-
199PhosphotyrosineLKKIYEDGD
HHHHHCCCC
19.49Phosphositeplus
Link-
199PhosphotyrosineLKKIYEDGD
HHHHHCCCC
19.49SysPTM
Link-
207Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DDDMKRTIN
CHHHHHHHH
54.08Phosphositeplus
Link-
209PhosphothreonineDMKRTINKA
HHHHHHHHH
24.31HPRD
Link-
209PhosphothreonineDMKRTINKA
HHHHHHHHH
24.31PhosphoELM
Link-
209PhosphothreonineDMKRTINKA
HHHHHHHHH
24.31Phosphositeplus
Link-
209Phosphothreonine.DMKRTINKA
HHHHHHHHH
24.31UniProtKB
Link-
212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RTINKAWVE
HHHHHHHHH
39.51Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SIAH1_HUMANphysical interactionMINT-18767MINT11389839
ARF6_HUMANphysical interactionEBI-1074486
intact17353931
S10A6_HUMANin vivoHPRD:07316HPRD12042313
S10A1_HUMANin vivoHPRD:07316HPRD12042313
S100B_HUMANin vitro
in vivo
HPRD:07316HPRD12042313
SKP1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:07316HPRD11389839
S100P_HUMANin vivoHPRD:07316HPRD12042313
S10AC_HUMANin vivoHPRD:07316HPRD12042313
SIAH1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:07316HPRD11389839
SIAH2_HUMANin vitro
yeast 2-hybrid
HPRD:07316HPRD11389839
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-8; LYS-19; LYS-85; LYS-118AND LYS-134, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-209, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures