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Protein Page:
CacyBP (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CacyBP a nuclear/cytoplasmic protein involved in calcium-dependent ubiquitination and proteosomal degradation of target proteins. A possible molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1). Interacts with proteins of the S100 family at physiological calcium concentrations. Component of some large E3 complexes and interacts directly with SIAH1, SIAH2 and SKP1A. 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. Two alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin conjugating system; Adaptor/scaffold
Chromosomal Location of Human Ortholog: 1q24-q25
Cellular Component: neuron projection; nuclear envelope lumen; cytoplasm; nucleolus; beta-catenin destruction complex; nucleus
Molecular Function: protein binding; protein homodimerization activity
Biological Process: positive regulation of DNA replication; cardiac muscle cell differentiation; aging
Reference #:  Q9HB71 (UniProtKB)
Alt. Names/Synonyms: CACYBP; calcyclin binding protein; Calcyclin-binding protein; CYBP; GIG5; growth-inhibiting gene 5 protein; hCacyBP; MGC87971; PNAS-107; RP1-102G20.6; S100A6-binding protein; S100A6BP; Siah-interacting protein; Siah-interacting protein (SIP); SIP
Gene Symbols: CACYBP
Molecular weight: 26,210 Da
Basal Isoelectric point: 8.28  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CacyBP

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: S141‑p
intracellular localization: S141‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 S3-p _____MAsEELQkDL
0 1 K8-ac MAsEELQkDLEEVkV
0 1 K8-sc MAsEELQkDLEEVkV
0 1 K14-ac QkDLEEVkVLLEkAT
1 0 K14 QkDLEEVKVLLEkAT
0 2 K14-ub QkDLEEVkVLLEkAT
0 2 K19-ac EVkVLLEkATRKRVR
0 1 K19-ub EVkVLLEkATRKRVR
0 2 S34-p DALTAEKsKIETEIk
0 5 K41-ub sKIETEIkNKMQQKs
0 2 S48-p kNKMQQKsQKKAELL
0 1 K59-ac AELLDNEkPAAVVAP
0 7 T68-p AAVVAPIttGytVKI
0 28 T69-p AVVAPIttGytVKIS
0 56 Y71-p VAPIttGytVKISNY
0 16 T72-p APIttGytVKISNYG
0 8 K85-ac YGWDQSDkFVKIyIT
0 1 K85-ub YGWDQSDkFVKIyIT
0 3 Y90-p SDkFVKIyITLTGVH
0 1 S112-p QVHFTERsFDLLVkN
0 1 K118-ac RsFDLLVkNLNGkSy
0 1 K118-ub RsFDLLVkNLNGkSy
0 4 K123-ub LVkNLNGkSySMIVN
0 2 Y125-p kNLNGkSySMIVNNL
0 2 K134-ac MIVNNLLkPISVEGs
1 0 S141-p kPISVEGsSkkVkTD
0 11 K143-ub ISVEGsSkkVkTDTV
0 6 K143-ac ISVEGsSkkVkTDTV
0 7 K144-ub SVEGsSkkVkTDTVL
0 24 K146-ub EGsSkkVkTDTVLIL
0 1 K178-ub KECKEKEkPsyDtEt
0 3 S180-p CKEKEkPsyDtEtDP
0 7 Y181-p KEKEkPsyDtEtDPs
0 6 T183-p KEkPsyDtEtDPsEG
0 1 T185-p kPsyDtEtDPsEGLM
0 1 S188-p yDtEtDPsEGLMNVL
0 1 K196-ub EGLMNVLkkIyEDGD
0 3 K197-ub GLMNVLkkIyEDGDD
0 244 Y199-p MNVLkkIyEDGDDDM
0 4 K207-ac EDGDDDMkRtINkAW
0 5 K207-ub EDGDDDMkRtINkAW
0 5 T209-p GDDDMkRtINkAWVE
0 30 K212-ub DMkRtINkAWVESRE
  mouse

 
S3 _____MASVLEELQK
K10 SVLEELQKDLEEVkV
K10 SVLEELQKDLEEVkV
K16 QKDLEEVKVLLEKST
K16-sm QKDLEEVkVLLEKST
K16-ub QKDLEEVkVLLEKST
K21 EVkVLLEKSTRKRLR
K21 EVkVLLEKSTRKRLR
S36 DTLTSEKSKIETELK
K43 SKIETELKNKMQQKS
S50 KNKMQQKSQKKPELD
K60 KPELDNEKPAAVVAP
T69 AAVVAPLTTGyTVKI
T70 AVVAPLTTGyTVKIS
Y72-p VAPLTTGyTVKISNY
T73 APLTTGyTVKISNYG
K86-ac YGWDQSDkFVKIYIT
K86 YGWDQSDKFVKIYIT
Y91 SDkFVKIYITLTGVH
S113 QVHFTERSFDLLVKN
K119 RSFDLLVKNLNGKNY
K119 RSFDLLVKNLNGKNY
K124 LVKNLNGKNYSMIVN
Y126 KNLNGKNYSMIVNNL
K135 MIVNNLLKPISVESS
S142 KPISVESSSkKVkTD
K144-ub ISVESSSkKVkTDTV
K144 ISVESSSKKVkTDTV
K145 SVESSSkKVkTDTVI
K147-ub ESSSkKVkTDTVIIL
K179 KECKEKEKPSYDTEA
S181 CKEKEKPSYDTEADP
Y182 KEKEKPSYDTEADPS
T184 KEKPSYDTEADPSEG
A186 KPSYDTEADPSEGLM
S189 YDTEADPSEGLMNVL
K197 EGLMNVLKkIyEDGD
K198-ub GLMNVLKkIyEDGDD
Y200-p MNVLKkIyEDGDDDM
K208 EDGDDDMKRTINkAW
K208 EDGDDDMKRTINkAW
T210 GDDDMKRTINkAWVE
K213-ub DMKRTINkAWVESRE
  rat

 
S3-p _____MAsALEELQK
K10 sALEELQKDLEEVKV
K10 sALEELQKDLEEVKV
K16 QKDLEEVKVLLEKST
K16 QKDLEEVKVLLEKST
K16 QKDLEEVKVLLEKST
K21 EVKVLLEKSTRKRLR
K21 EVKVLLEKSTRKRLR
S36 DTLTNEKSKIETELR
R43 SKIETELRNKMQQKS
S50 RNKMQQKSQKKPEFD
K60 KPEFDNEKPAAVVAP
T69 AAVVAPLTTGYTVKI
T70 AVVAPLTTGYTVKIS
Y72 VAPLTTGYTVKISNY
T73 APLTTGYTVKISNYG
K86-ac YGWDQSDkFVKIYIT
K86 YGWDQSDKFVKIYIT
Y91 SDkFVKIYITLTGVH
S113 QVHFTERSFDLLVKN
K119 RSFDLLVKNLNGKNY
K119 RSFDLLVKNLNGKNY
K124 LVKNLNGKNYSMIVN
Y126 KNLNGKNYSMIVNNL
K135 MIVNNLLKPISVESS
S142 KPISVESSSKKVKTD
K144 ISVESSSKKVKTDTV
K144 ISVESSSKKVKTDTV
K145 SVESSSKKVKTDTVI
K147 ESSSKKVKTDTVIIL
K179 KECKEKEKPSYDTEA
S181 CKEKEKPSYDTEADP
Y182 KEKEKPSYDTEADPS
T184 KEKPSYDTEADPSEG
A186 KPSYDTEADPSEGLM
S189 YDTEADPSEGLMNVL
K197 EGLMNVLKKIYEDGD
K198 GLMNVLKKIYEDGDD
Y200 MNVLKKIYEDGDDDM
K208 EDGDDDMKRTINKAW
K208 EDGDDDMKRTINKAW
T210 GDDDMKRTINKAWVE
K213 DMKRTINKAWVESRE
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