ID   Q6NVY0_HUMAN            Unreviewed;       228 AA.
AC   Q6NVY0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   22-FEB-2023, entry version 89.
DE   RecName: Full=Calcyclin-binding protein {ECO:0000256|ARBA:ARBA00015702};
GN   Name=CACYBP {ECO:0000313|EMBL:AAH67823.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAH67823.1};
RN   [1] {ECO:0000313|EMBL:AAH67823.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAH67823.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in calcium-dependent ubiquitination and
CC       subsequent proteasomal degradation of target proteins. Probably serves
CC       as a molecular bridge in ubiquitin E3 complexes. Participates in the
CC       ubiquitin-mediated degradation of beta-catenin (CTNNB1).
CC       {ECO:0000256|ARBA:ARBA00025145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; BC067823; AAH67823.1; -; mRNA.
DR   AlphaFoldDB; Q6NVY0; -.
DR   SMR; Q6NVY0; -.
DR   IntAct; Q6NVY0; 1.
DR   PeptideAtlas; Q6NVY0; -.
DR   ChiTaRS; CACYBP; human.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044548; F:S100 protein binding; IEA:InterPro.
DR   GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   CDD; cd06468; p23_CacyBP; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   InterPro; IPR037201; CacyBP_N.
DR   InterPro; IPR037893; CS_CacyBP.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR007699; SGS_dom.
DR   InterPro; IPR015120; Siah-Interact_N.
DR   PANTHER; PTHR13164:SF3; CALCYCLIN-BINDING PROTEIN; 1.
DR   PANTHER; PTHR13164; CALICYLIN BINDING PROTEIN; 1.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF05002; SGS; 1.
DR   Pfam; PF09032; Siah-Interact_N; 1.
DR   SUPFAM; SSF140106; Calcyclin-binding protein-like; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS51203; CS; 1.
DR   PROSITE; PS51048; SGS; 1.
PE   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          73..167
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   DOMAIN          151..228
FT                   /note="SGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51048"
FT   COILED          3..57
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   228 AA;  26182 MW;  88C822FB16CA7F89 CRC64;
     MASEELQKDL EEVKVLLEKA TRKRVRDALT AEKSKIETEI KNKMQQKSQK KAELLDNEKP
     AAVVAPITTG YTVKISNYGW DQSDKFVKIY ITLTGVHQVP TENVQVHFTE RSFDLLVKNL
     NGKSYSMIVN NLLKPISVEG SSKKVKTDTV LILCRKKVEN TRWDYLTQVE KECKEKEKPS
     YDTETDPSEG LMNVLKKIYE DGDDDMKQTI NKAWVESREK QAKGDTEF
//