Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9CXW3

- CYBP_MOUSE

UniProt

Q9CXW3 - CYBP_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Calcyclin-binding protein

Gene

Cacybp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

  1. aging Source: Ensembl
  2. cardiac muscle cell differentiation Source: Ensembl
  3. cellular response to calcium ion Source: Ensembl
  4. negative regulation of cell death Source: Ensembl
  5. positive regulation of DNA replication Source: Ensembl
  6. response to growth hormone Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Calcyclin-binding protein
Short name:
CacyBP
Alternative name(s):
Siah-interacting protein
Gene namesi
Name:Cacybp
Synonyms:Sip
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1270839. Cacybp.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication
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.

GO - Cellular componenti

  1. beta-catenin destruction complex Source: UniProtKB
  2. cell body Source: Ensembl
  3. cytoplasm Source: MGI
  4. extracellular vesicular exosome Source: Ensembl
  5. neuron projection Source: Ensembl
  6. nuclear envelope lumen Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 229228Calcyclin-binding proteinPRO_0000185390Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei10 – 101N6-acetyllysineBy similarity
Modified residuei21 – 211N6-acetyllysineBy similarity
Modified residuei86 – 861N6-acetyllysineBy similarity
Modified residuei119 – 1191N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated on serine residues. Phosphorylated upon induction by RA or at high calcium concentrations.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9CXW3.
PaxDbiQ9CXW3.
PRIDEiQ9CXW3.

2D gel databases

REPRODUCTION-2DPAGEQ9CXW3.

PTM databases

PhosphoSiteiQ9CXW3.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ9CXW3.
CleanExiMM_CACYBP.
GenevestigatoriQ9CXW3.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
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.

Protein-protein interaction databases

BioGridi198445. 8 interactions.
IntActiQ9CXW3. 11 interactions.
MINTiMINT-238999.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 2120Combined sources
Turni22 – 265Combined sources
Helixi27 – 4721Combined sources
Helixi192 – 2009Combined sources
Helixi207 – 21610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YSMNMR-A1-77[»]
2JTTNMR-C/D189-219[»]
DisProtiDP00226.
ProteinModelPortaliQ9CXW3.
SMRiQ9CXW3. Positions 1-55, 62-181, 189-219.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CXW3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 16895CSPROSITE-ProRule annotationAdd
BLAST
Domaini169 – 22961SGSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 8180Interaction with SIAH1By similarityAdd
BLAST
Regioni74 – 229156Interaction with SKP1By similarityAdd
BLAST
Regioni155 – 22975Interaction with S100A6Add
BLAST

Sequence similaritiesi

Contains 1 CS domain.PROSITE-ProRule annotation
Contains 1 SGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG247905.
GeneTreeiENSGT00390000016470.
HOGENOMiHOG000238284.
HOVERGENiHBG003242.
InParanoidiQ9CXW3.
KOiK04507.
OMAiVNFTERS.
OrthoDBiEOG7K9K4J.
PhylomeDBiQ9CXW3.
TreeFamiTF323891.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007699. SGS.
IPR015120. Siah-Interact_N.
[Graphical view]
PfamiPF04969. CS. 1 hit.
PF05002. SGS. 1 hit.
PF09032. Siah-Interact_N. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
PS51048. SGS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CXW3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASVLEELQK DLEEVKVLLE KSTRKRLRDT LTSEKSKIET ELKNKMQQKS
60 70 80 90 100
QKKPELDNEK PAAVVAPLTT GYTVKISNYG WDQSDKFVKI YITLTGVHQV
110 120 130 140 150
PTENVQVHFT ERSFDLLVKN LNGKNYSMIV NNLLKPISVE SSSKKVKTDT
160 170 180 190 200
VIILCRKKAE NTRWDYLTQV EKECKEKEKP SYDTEADPSE GLMNVLKKIY
210 220
EDGDDDMKRT INKAWVESRE KQAREDTEF
Length:229
Mass (Da):26,510
Last modified:June 1, 2001 - v1
Checksum:i2B04B54D0054ACE0
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97327 mRNA. Translation: AAC16757.1. Different initiation.
AK013924 mRNA. No translation available.
BC025948 mRNA. Translation: AAH25948.1.
CCDSiCCDS15406.1.
RefSeqiNP_033916.1. NM_009786.2.
UniGeneiMm.10702.

Genome annotation databases

EnsembliENSMUST00000014370; ENSMUSP00000014370; ENSMUSG00000014226.
GeneIDi12301.
KEGGimmu:12301.
UCSCiuc007deg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U97327 mRNA. Translation: AAC16757.1 . Different initiation.
AK013924 mRNA. No translation available.
BC025948 mRNA. Translation: AAH25948.1 .
CCDSi CCDS15406.1.
RefSeqi NP_033916.1. NM_009786.2.
UniGenei Mm.10702.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YSM NMR - A 1-77 [» ]
2JTT NMR - C/D 189-219 [» ]
DisProti DP00226.
ProteinModelPortali Q9CXW3.
SMRi Q9CXW3. Positions 1-55, 62-181, 189-219.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198445. 8 interactions.
IntActi Q9CXW3. 11 interactions.
MINTi MINT-238999.

PTM databases

PhosphoSitei Q9CXW3.

2D gel databases

REPRODUCTION-2DPAGE Q9CXW3.

Proteomic databases

MaxQBi Q9CXW3.
PaxDbi Q9CXW3.
PRIDEi Q9CXW3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000014370 ; ENSMUSP00000014370 ; ENSMUSG00000014226 .
GeneIDi 12301.
KEGGi mmu:12301.
UCSCi uc007deg.2. mouse.

Organism-specific databases

CTDi 27101.
MGIi MGI:1270839. Cacybp.

Phylogenomic databases

eggNOGi NOG247905.
GeneTreei ENSGT00390000016470.
HOGENOMi HOG000238284.
HOVERGENi HBG003242.
InParanoidi Q9CXW3.
KOi K04507.
OMAi VNFTERS.
OrthoDBi EOG7K9K4J.
PhylomeDBi Q9CXW3.
TreeFami TF323891.

Miscellaneous databases

EvolutionaryTracei Q9CXW3.
NextBioi 280826.
PROi Q9CXW3.
SOURCEi Search...

Gene expression databases

Bgeei Q9CXW3.
CleanExi MM_CACYBP.
Genevestigatori Q9CXW3.

Family and domain databases

Gene3Di 2.60.40.790. 1 hit.
InterProi IPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007699. SGS.
IPR015120. Siah-Interact_N.
[Graphical view ]
Pfami PF04969. CS. 1 hit.
PF05002. SGS. 1 hit.
PF09032. Siah-Interact_N. 1 hit.
[Graphical view ]
SUPFAMi SSF49764. SSF49764. 1 hit.
PROSITEi PS51203. CS. 1 hit.
PS51048. SGS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCYBP_MOUSE
AccessioniPrimary (citable) accession number: Q9CXW3
Secondary accession number(s): O70140
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3