Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9CXW3 (CYBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcyclin-binding protein

Short name=CacyBP
Alternative name(s):
Siah-interacting protein
Gene names
Name:Cacybp
Synonyms:Sip
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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) By similarity.

Subunit structure

Monomer or homodimer. Component of some large E3 complex at least composed of UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts directly with SIAH1, SIAH2 and SKP1 By similarity. Interacts with proteins of the S100 family S100A1, S100A6, S100B, S100P and S100A12 in a calcium-dependent manner By similarity. Ref.1 Ref.4 Ref.6 Ref.7

Subcellular location

Nucleus. Cytoplasm. Note: Cytoplasmic in unstimulated cultured neurons. Upon increase of calcium, it localizes to a ring around the nucleus. In neuroblastoma cells, after a Retinoic acid (RA) induction and calcium increase, it localizes in both the nucleus and cytoplasm. The nuclear and perinuclear fractions may be phosphorylated. Ref.5

Tissue specificity

Highly expressed in brain and EAT cells. Expressed at low level in heart, muscle, and at very low level in the liver, spleen, lung, kidney and stomach. Ref.1

Post-translational modification

Phosphorylated on serine residues. Phosphorylated upon induction by RA or at high calcium concentrations. Ref.5

Sequence similarities

Contains 1 CS domain.

Contains 1 SGS domain.

Sequence caution

The sequence AAC16757.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

S100A1P026394EBI-767146,EBI-6477285From a different organism.
S100a6P140694EBI-767146,EBI-6478740
S100BP026384EBI-767146,EBI-458452From a different organism.
S100PP258152EBI-767146,EBI-743700From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 229228Calcyclin-binding protein
PRO_0000185390

Regions

Domain74 – 16895CS
Domain169 – 22961SGS
Region2 – 8180Interaction with SIAH1 By similarity
Region74 – 229156Interaction with SKP1 By similarity
Region155 – 22975Interaction with S100A6

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue101N6-acetyllysine By similarity
Modified residue211N6-acetyllysine By similarity
Modified residue861N6-acetyllysine By similarity
Modified residue1191N6-acetyllysine By similarity

Secondary structure

......... 229
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9CXW3 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2B04B54D0054ACE0

FASTA22926,510
        10         20         30         40         50         60 
MASVLEELQK DLEEVKVLLE KSTRKRLRDT LTSEKSKIET ELKNKMQQKS QKKPELDNEK 

        70         80         90        100        110        120 
PAAVVAPLTT GYTVKISNYG WDQSDKFVKI YITLTGVHQV PTENVQVHFT ERSFDLLVKN 

       130        140        150        160        170        180 
LNGKNYSMIV NNLLKPISVE SSSKKVKTDT VIILCRKKAE NTRWDYLTQV EKECKEKEKP 

       190        200        210        220 
SYDTEADPSE GLMNVLKKIY EDGDDDMKRT INKAWVESRE KQAREDTEF 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a mouse brain cDNA encoding a novel protein target of calcyclin."
Filipek A., Kuznicki J.
J. Neurochem. 70:1793-1798(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-22; 73-85 AND 222-229, TISSUE SPECIFICITY, INTERACTION WITH S100A6.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Characterization of the interaction of calcyclin (S100A6) and calcyclin-binding protein."
Nowotny M., Bhattacharya S., Filipek A., Krezel A.M., Chazin W., Kuznicki J.
J. Biol. Chem. 275:31178-31182(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH S100A6.
[5]"Ca2+-dependent translocation of the calcyclin-binding protein in neurons and neuroblastoma NB-2a cells."
Filipek A., Jastrzebska B., Nowotny M., Kwiatkowska K., Hetman M., Surmacz L., Wyroba E., Kuznicki J.
J. Biol. Chem. 277:21103-21109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[6]"The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies."
Bhattacharya S., Lee Y.-T., Michowski W., Jastrzebska B., Filipek A., Kuznicki J., Chazin W.J.
Biochemistry 44:9462-9471(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-77, INTERACTION WITH SKP1 AND S100A6, SUBUNIT.
[7]"Structure of the S100A6 complex with a fragment from the C-terminal domain of Siah-1 interacting protein: a novel mode for S100 protein target recognition."
Lee Y.-T., Dimitrova Y.N., Schneider G., Ridenour W.B., Bhattacharya S., Soss S.E., Caprioli R.M., Filipek A., Chazin W.J.
Biochemistry 47:10921-10932(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 189-219 IN COMPLEX WITH S100A6, INTERACTION WITH S100A6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U97327 mRNA. Translation: AAC16757.1. Different initiation.
AK013924 mRNA. No translation available.
BC025948 mRNA. Translation: AAH25948.1.
CCDSCCDS15406.1.
RefSeqNP_033916.1. NM_009786.2.
UniGeneMm.10702.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YSMNMR-A1-77[»]
2JTTNMR-C/D189-219[»]
DisProtDP00226.
ProteinModelPortalQ9CXW3.
SMRQ9CXW3. Positions 1-55, 62-181, 189-219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198445. 8 interactions.
IntActQ9CXW3. 11 interactions.
MINTMINT-238999.

PTM databases

PhosphoSiteQ9CXW3.

2D gel databases

REPRODUCTION-2DPAGEQ9CXW3.

Proteomic databases

MaxQBQ9CXW3.
PaxDbQ9CXW3.
PRIDEQ9CXW3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000014370; ENSMUSP00000014370; ENSMUSG00000014226.
GeneID12301.
KEGGmmu:12301.
UCSCuc007deg.2. mouse.

Organism-specific databases

CTD27101.
MGIMGI:1270839. Cacybp.

Phylogenomic databases

eggNOGNOG247905.
GeneTreeENSGT00390000016470.
HOGENOMHOG000238284.
HOVERGENHBG003242.
InParanoidQ9CXW3.
KOK04507.
OMAVNFTERS.
OrthoDBEOG7K9K4J.
PhylomeDBQ9CXW3.
TreeFamTF323891.

Gene expression databases

BgeeQ9CXW3.
CleanExMM_CACYBP.
GenevestigatorQ9CXW3.

Family and domain databases

Gene3D2.60.40.790. 1 hit.
InterProIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007699. SGS.
IPR015120. Siah-Interact_N.
[Graphical view]
PfamPF04969. CS. 1 hit.
PF05002. SGS. 1 hit.
PF09032. Siah-Interact_N. 1 hit.
[Graphical view]
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS51203. CS. 1 hit.
PS51048. SGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9CXW3.
NextBio280826.
PROQ9CXW3.
SOURCESearch...

Entry information

Entry nameCYBP_MOUSE
AccessionPrimary (citable) accession number: Q9CXW3
Secondary accession number(s): O70140
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot