Full text data of CAND1
CAND1
(KIAA0829, TIP120, TIP120A)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Cullin-associated NEDD8-dissociated protein 1 (Cullin-associated and neddylation-dissociated protein 1; TBP-interacting protein of 120 kDa A; TBP-interacting protein 120A; p120 CAND1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cullin-associated NEDD8-dissociated protein 1 (Cullin-associated and neddylation-dissociated protein 1; TBP-interacting protein of 120 kDa A; TBP-interacting protein 120A; p120 CAND1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00100160
IPI00100160 Hypothetical protein FLJ14877 binding soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00100160 Hypothetical protein FLJ14877 binding soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q86VP6
ID CAND1_HUMAN Reviewed; 1230 AA.
AC Q86VP6; B2RAU3; O94918; Q6PIY4; Q8NDJ4; Q96JZ9; Q96T19; Q9BTC4;
read moreAC Q9H0G2; Q9P0H7; Q9UF85;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Cullin-associated NEDD8-dissociated protein 1;
DE AltName: Full=Cullin-associated and neddylation-dissociated protein 1;
DE AltName: Full=TBP-interacting protein of 120 kDa A;
DE Short=TBP-interacting protein 120A;
DE AltName: Full=p120 CAND1;
GN Name=CAND1; Synonyms=KIAA0829, TIP120, TIP120A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP VAL-952.
RC TISSUE=Cervix, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-14 AND 374-382, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Ramsay A., Leung H.Y.;
RL Submitted (MAR-2009) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 2-14; 535-548; 668-679; 730-743; 859-873; 958-969
RP AND 983-990, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
RP AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [10]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND IDENTIFICATION IN A COMPLEX
RP WITH CUL1 AND RBX1.
RX PubMed=12504026; DOI=10.1016/S1097-2765(02)00784-0;
RA Zheng J., Yang X., Harrell J.M., Ryzhikov S., Shim E.-H.,
RA Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H.;
RT "CAND1 binds to unneddylated CUL1 and regulates the formation of SCF
RT ubiquitin E3 ligase complex.";
RL Mol. Cell 10:1519-1526(2002).
RN [11]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1 AND RBX1, AND
RP INTERACTION WITH UNNEDDYLATED CUL1; CUL4A AND CUL5.
RX PubMed=12504025; DOI=10.1016/S1097-2765(02)00783-9;
RA Liu J., Furukawa M., Matsumoto T., Xiong Y.;
RT "NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of
RT CUL1-SKP1 binding and SCF ligases.";
RL Mol. Cell 10:1511-1518(2002).
RN [12]
RP FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B AND RBX1,
RP AND MASS SPECTROMETRY.
RX PubMed=12609982; DOI=10.1074/jbc.M213070200;
RA Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.;
RT "TIP120A associates with cullins and modulates ubiquitin ligase
RT activity.";
RL J. Biol. Chem. 278:15905-15910(2003).
RN [13]
RP FUNCTION, AND INTERACTION WITH CUL3.
RX PubMed=16449638; DOI=10.1128/MCB.26.4.1235-1244.2006;
RA Lo S.C., Hannink M.;
RT "CAND1-mediated substrate adaptor recycling is required for efficient
RT repression of Nrf2 by Keap1.";
RL Mol. Cell. Biol. 26:1235-1244(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-971, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP INDUCTION.
RX PubMed=20820187; DOI=10.1038/pcan.2010.32;
RA Murata T., Takayama K., Katayama S., Urano T., Horie-Inoue K.,
RA Ikeda K., Takahashi S., Kawazu C., Hasegawa A., Ouchi Y., Homma Y.,
RA Hayashizaki Y., Inoue S.;
RT "miR-148a is an androgen-responsive microRNA that promotes LNCaP
RT prostate cell growth by repressing its target CAND1 expression.";
RL Prostate Cancer Prostatic Dis. 13:356-361(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP INTERACTION WITH CUL2.
RX PubMed=21778237; DOI=10.1074/jbc.M111.278408;
RA Mao X., Gluck N., Chen B., Starokadomskyy P., Li H., Maine G.N.,
RA Burstein E.;
RT "COMMD1 (copper metabolism MURR1 domain-containing protein 1)
RT regulates Cullin RING ligases by preventing CAND1 (Cullin-associated
RT Nedd8-dissociated protein 1) binding.";
RL J. Biol. Chem. 286:32355-32365(2011).
RN [21]
RP FUNCTION, INTERACTION WITH CUL2; CUL3; CUL4A AND CUL5, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21249194; DOI=10.1371/journal.pone.0016071;
RA Chua Y.S., Boh B.K., Ponyeam W., Hagen T.;
RT "Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo.";
RL PLoS ONE 6:E16071-E16071(2011).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP FUNCTION, AND REACTION MECHANISM.
RX PubMed=23453757; DOI=10.1016/j.cell.2013.02.024;
RA Pierce N.W., Lee J.E., Liu X., Sweredoski M.J., Graham R.L.,
RA Larimore E.A., Rome M., Zheng N., Clurman B.E., Hess S., Shan S.O.,
RA Deshaies R.J.;
RT "Cand1 promotes assembly of new SCF complexes through dynamic exchange
RT of F box proteins.";
RL Cell 153:206-215(2013).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CUL1 AND RBX1.
RX PubMed=15537541; DOI=10.1016/j.cell.2004.10.019;
RA Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J.,
RA Xiong Y., Zheng N.;
RT "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory
RT mechanisms for the assembly of the multisubunit cullin-dependent
RT ubiquitin ligases.";
RL Cell 119:517-528(2004).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEX WITH CUL4B AND RBX1.
RX PubMed=22118460; DOI=10.1016/j.cell.2011.10.035;
RA Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M.,
RA Faty M., Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S.,
RA Gut H., Sugasawa K., Thoma N.H.;
RT "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture,
RT targeting, and activation.";
RL Cell 147:1024-1039(2011).
CC -!- FUNCTION: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3
CC ubiquitin ligase complexes that promotes the exchange of the
CC substrate-recognition F-box subunit in SCF complexes, thereby
CC playing a key role in the cellular repertoire of SCF complexes.
CC Acts as a F-box protein exchange factor. The exchange activity of
CC CAND1 is coupled with cycles of neddylation conjugation: in the
CC deneddylated state, cullin-binding CAND1 binds CUL1-RBX1,
CC increasing dissociation of the SCF complex and promoting exchange
CC of the F-box protein. Probably plays a similar role in other
CC cullin-RING E3 ubiquitin ligase complexes.
CC -!- SUBUNIT: Interacts with TBP (By similarity). Part of a complex
CC that contains CUL1 and RBX1. Interacts with unneddylated cullins:
CC interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5. Does not
CC bind neddylated CUL1. Interaction with cullins is abolished in
CC presence of COMMD1, which antagonizes with CAND1 for interacting
CC with cullins.
CC -!- INTERACTION:
CC Q13616:CUL1; NbExp=19; IntAct=EBI-456077, EBI-359390;
CC Q13617:CUL2; NbExp=3; IntAct=EBI-456077, EBI-456179;
CC Q13618:CUL3; NbExp=2; IntAct=EBI-456077, EBI-456129;
CC Q13619:CUL4A; NbExp=3; IntAct=EBI-456077, EBI-456106;
CC Q13620:CUL4B; NbExp=3; IntAct=EBI-456077, EBI-456067;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86VP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VP6-2; Sequence=VSP_013948;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q86VP6-3; Sequence=VSP_013947, VSP_013949, VSP_013950;
CC Note=No experimental confirmation available;
CC -!- INDUCTION: Repressed by miR-148a.
CC -!- MISCELLANEOUS: A model has been proposed to explain the mechanisms
CC of cullin-RING E3 ubiquitin ligase complexes assembly. According
CC to this hypothesis, cullin-RING E3 ubiquitin ligase complexes
CC exist in a 'stable' active state when saturated with substrate,
CC occluding access to deneddylation by the COP9 signalosome (CSN)
CC complex. The neddylation-conjugated cullin-RING E3 ubiquitin
CC ligase complexes mediate ubiquitination of substrates and can
CC recruit downstream factors involved in substrate degradation.
CC Depletion of the substrate promotes the ability of CSN to bind the
CC cullin-RING E3 ubiquitin ligase complex and mediate deneddylation.
CC In this 'intermediate' deneddylated state, the complex can bind
CC CAND1 and enter the 'exchange' state, resulting in high increase
CC in dissociation rate of the substrate-recognition subunit. The
CC resulting CAND1-cullin-RING complex rapidly assembles with another
CC available substrate-recognition subunit to form an unstable
CC ternary intermediate and yield a new cullin-RING E3 ubiquitin
CC ligase complex. Subsequent neddylation of the cullin, which is
CC stabilized by substrate, completes the cycle (PubMed:23453757).
CC -!- SIMILARITY: Belongs to the CAND family.
CC -!- SIMILARITY: Contains 27 HEAT repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74852.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB55090.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB020636; BAA74852.2; ALT_INIT; mRNA.
DR EMBL; AF157326; AAF67492.1; -; mRNA.
DR EMBL; AL133560; CAB63714.1; -; mRNA.
DR EMBL; AL136810; CAB66744.1; -; mRNA.
DR EMBL; AL833880; CAD38737.1; -; mRNA.
DR EMBL; CH471054; EAW97172.1; -; Genomic_DNA.
DR EMBL; BC004232; AAH04232.1; -; mRNA.
DR EMBL; BC026220; AAH26220.1; -; mRNA.
DR EMBL; BC050341; AAH50341.1; -; mRNA.
DR EMBL; AK027404; BAB55090.1; ALT_INIT; mRNA.
DR EMBL; AK027783; BAB55365.1; -; mRNA.
DR EMBL; AK314358; BAG36990.1; -; mRNA.
DR PIR; T43441; T43441.
DR RefSeq; NP_060918.2; NM_018448.3.
DR UniGene; Hs.546407; -.
DR PDB; 1U6G; X-ray; 3.10 A; C=1-1230.
DR PDB; 4A0C; X-ray; 3.80 A; A/B=1-1230.
DR PDBsum; 1U6G; -.
DR PDBsum; 4A0C; -.
DR ProteinModelPortal; Q86VP6; -.
DR DIP; DIP-31608N; -.
DR IntAct; Q86VP6; 15.
DR MINT; MINT-4999459; -.
DR PhosphoSite; Q86VP6; -.
DR DMDM; 67460541; -.
DR PaxDb; Q86VP6; -.
DR PRIDE; Q86VP6; -.
DR DNASU; 55832; -.
DR Ensembl; ENST00000544619; ENSP00000444089; ENSG00000111530.
DR Ensembl; ENST00000545606; ENSP00000442318; ENSG00000111530.
DR GeneID; 55832; -.
DR KEGG; hsa:55832; -.
DR UCSC; uc001stn.2; human.
DR CTD; 55832; -.
DR GeneCards; GC12P067663; -.
DR HGNC; HGNC:30688; CAND1.
DR MIM; 607727; gene.
DR neXtProt; NX_Q86VP6; -.
DR PharmGKB; PA142672207; -.
DR eggNOG; NOG278162; -.
DR HOVERGEN; HBG053467; -.
DR InParanoid; Q86VP6; -.
DR KO; K17263; -.
DR OMA; AIACMGQ; -.
DR OrthoDB; EOG77HDCZ; -.
DR PhylomeDB; Q86VP6; -.
DR ChiTaRS; CAND1; human.
DR EvolutionaryTrace; Q86VP6; -.
DR GeneWiki; CAND1; -.
DR GenomeRNAi; 55832; -.
DR NextBio; 61049; -.
DR PRO; PR:Q86VP6; -.
DR ArrayExpress; Q86VP6; -.
DR Bgee; Q86VP6; -.
DR Genevestigator; Q86VP6; -.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0010265; P:SCF complex assembly; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013932; TATA-bd_TIP120.
DR Pfam; PF08623; TIP120; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1230 Cullin-associated NEDD8-dissociated
FT protein 1.
FT /FTId=PRO_0000089293.
FT REPEAT 2 39 HEAT 1.
FT REPEAT 44 81 HEAT 2.
FT REPEAT 83 119 HEAT 3.
FT REPEAT 131 165 HEAT 4.
FT REPEAT 171 208 HEAT 5.
FT REPEAT 210 247 HEAT 6.
FT REPEAT 248 282 HEAT 7.
FT REPEAT 289 366 HEAT 8.
FT REPEAT 370 407 HEAT 9.
FT REPEAT 424 467 HEAT 10.
FT REPEAT 471 510 HEAT 11.
FT REPEAT 515 552 HEAT 12.
FT REPEAT 563 602 HEAT 13.
FT REPEAT 606 643 HEAT 14.
FT REPEAT 646 683 HEAT 15.
FT REPEAT 688 725 HEAT 16.
FT REPEAT 729 768 HEAT 17.
FT REPEAT 770 808 HEAT 18.
FT REPEAT 809 845 HEAT 19.
FT REPEAT 852 889 HEAT 20.
FT REPEAT 890 927 HEAT 21.
FT REPEAT 928 960 HEAT 22.
FT REPEAT 961 998 HEAT 23.
FT REPEAT 1002 1039 HEAT 24.
FT REPEAT 1043 1097 HEAT 25.
FT REPEAT 1099 1133 HEAT 26.
FT REPEAT 1140 1189 HEAT 27.
FT COMPBIAS 314 344 Asp-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 55 55 N6-acetyllysine.
FT MOD_RES 335 335 Phosphoserine.
FT MOD_RES 971 971 N6-acetyllysine.
FT VAR_SEQ 1 157 Missing (in isoform 3).
FT /FTId=VSP_013947.
FT VAR_SEQ 458 625 Missing (in isoform 2).
FT /FTId=VSP_013948.
FT VAR_SEQ 549 560 VIRPLDQPSSFD -> AHHMPEAQWLRL (in isoform
FT 3).
FT /FTId=VSP_013949.
FT VAR_SEQ 561 1230 Missing (in isoform 3).
FT /FTId=VSP_013950.
FT VARIANT 803 803 V -> A (in dbSNP:rs12580996).
FT /FTId=VAR_054041.
FT VARIANT 952 952 A -> V (in dbSNP:rs17854618).
FT /FTId=VAR_025327.
FT CONFLICT 272 272 R -> K (in Ref. 7; BAB55365).
FT CONFLICT 457 457 M -> I (in Ref. 7; BAB55090).
FT CONFLICT 606 606 S -> P (in Ref. 3; AAF67492).
FT CONFLICT 609 609 P -> S (in Ref. 3; AAF67492).
FT CONFLICT 1047 1047 T -> S (in Ref. 3; AAF67492).
FT CONFLICT 1177 1177 M -> T (in Ref. 7; BAB55090).
FT HELIX 6 14
FT HELIX 20 33
FT STRAND 35 37
FT HELIX 45 56
FT HELIX 62 76
FT HELIX 81 94
FT STRAND 98 100
FT HELIX 101 116
FT HELIX 127 142
FT HELIX 148 164
FT TURN 170 172
FT HELIX 173 180
FT HELIX 181 185
FT HELIX 189 202
FT TURN 203 205
FT HELIX 214 224
FT HELIX 234 244
FT HELIX 247 249
FT HELIX 256 264
FT TURN 269 271
FT HELIX 272 284
FT HELIX 291 301
FT HELIX 348 361
FT HELIX 368 372
FT TURN 373 375
FT HELIX 376 380
FT STRAND 386 388
FT HELIX 389 405
FT HELIX 424 431
FT HELIX 434 442
FT HELIX 448 464
FT TURN 466 469
FT HELIX 470 472
FT HELIX 473 483
FT STRAND 487 489
FT HELIX 491 506
FT HELIX 510 513
FT HELIX 514 517
FT TURN 518 520
FT HELIX 521 528
FT HELIX 533 550
FT STRAND 553 555
FT HELIX 562 576
FT STRAND 579 581
FT HELIX 583 599
FT HELIX 601 603
FT HELIX 607 618
FT STRAND 621 623
FT HELIX 624 635
FT HELIX 645 658
FT HELIX 664 680
FT HELIX 687 694
FT HELIX 698 700
FT HELIX 706 719
FT HELIX 724 729
FT TURN 730 734
FT HELIX 735 742
FT HELIX 749 763
FT HELIX 772 779
FT TURN 781 785
FT HELIX 793 809
FT HELIX 815 818
FT TURN 819 824
FT TURN 826 829
FT HELIX 832 848
FT HELIX 856 863
FT HELIX 864 866
FT HELIX 870 886
FT HELIX 888 900
FT HELIX 903 905
FT HELIX 906 918
FT TURN 923 925
FT HELIX 926 936
FT HELIX 947 960
FT HELIX 963 965
FT HELIX 967 970
FT TURN 971 973
FT STRAND 974 977
FT HELIX 979 988
FT HELIX 990 992
FT HELIX 1001 1007
FT TURN 1009 1014
FT STRAND 1015 1019
FT HELIX 1021 1036
FT HELIX 1038 1040
FT HELIX 1042 1044
FT HELIX 1045 1054
FT HELIX 1060 1062
FT STRAND 1063 1068
FT STRAND 1071 1076
FT HELIX 1079 1094
FT STRAND 1098 1100
FT HELIX 1102 1111
FT HELIX 1117 1132
FT HELIX 1136 1139
FT TURN 1140 1145
FT HELIX 1146 1154
FT HELIX 1163 1182
FT STRAND 1190 1194
FT HELIX 1200 1208
SQ SEQUENCE 1230 AA; 136376 MW; FE344558F72D79D8 CRC64;
MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILKLLEDK
NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE QLRDISSIGL KTVIGELPPA
SSGSALAANV CKKITGRLTS AIAKQEDVSV QLEALDIMAD MLSRQGGLLV NFHPSILTCL
LPQLTSPRLA VRKRTIIALG HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA
ISRQAGHRIG EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI
CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR RAAAKCLDAV
VSTRHEMLPE FYKTVSPALI SRFKEREENV KADVFHAYLS LLKQTRPVQS WLCDPDAMEQ
GETPLTMLQS QVPNIVKALH KQMKEKSVKT RQCCFNMLTE LVNVLPGALT QHIPVLVPGI
IFSLNDKSSS SNLKIDALSC LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL
LVTQQLVKVI RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL
GDNLGSDLPN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE GVPILASFLR
KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL ISESDMHVSQ MAISFLTTLA
KVYPSSLSKI SGSILNELIG LVRSPLLQGG ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT
GPVYSQSTAL THKQSYYSIA KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL
SLGEVGHHID LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT
SQPKRQYLLL HSLKEIISSA SVVGLKPYVE NIWALLLKHC ECAEEGTRNV VAECLGKLTL
IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI DPLLKNCIGD FLKTLEDPDL
NVRRVALVTF NSAAHNKPSL IRDLLDTVLP HLYNETKVRK ELIREVEMGP FKHTVDDGLD
IRKAAFECMY TLLDSCLDRL DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ
RLDRLVEPLR ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS
QISSNPELAA IFESIQKDSS STNLESMDTS
//
ID CAND1_HUMAN Reviewed; 1230 AA.
AC Q86VP6; B2RAU3; O94918; Q6PIY4; Q8NDJ4; Q96JZ9; Q96T19; Q9BTC4;
read moreAC Q9H0G2; Q9P0H7; Q9UF85;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Cullin-associated NEDD8-dissociated protein 1;
DE AltName: Full=Cullin-associated and neddylation-dissociated protein 1;
DE AltName: Full=TBP-interacting protein of 120 kDa A;
DE Short=TBP-interacting protein 120A;
DE AltName: Full=p120 CAND1;
GN Name=CAND1; Synonyms=KIAA0829, TIP120, TIP120A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP VAL-952.
RC TISSUE=Cervix, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-14 AND 374-382, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Ramsay A., Leung H.Y.;
RL Submitted (MAR-2009) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 2-14; 535-548; 668-679; 730-743; 859-873; 958-969
RP AND 983-990, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
RP AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [10]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND IDENTIFICATION IN A COMPLEX
RP WITH CUL1 AND RBX1.
RX PubMed=12504026; DOI=10.1016/S1097-2765(02)00784-0;
RA Zheng J., Yang X., Harrell J.M., Ryzhikov S., Shim E.-H.,
RA Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H.;
RT "CAND1 binds to unneddylated CUL1 and regulates the formation of SCF
RT ubiquitin E3 ligase complex.";
RL Mol. Cell 10:1519-1526(2002).
RN [11]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1 AND RBX1, AND
RP INTERACTION WITH UNNEDDYLATED CUL1; CUL4A AND CUL5.
RX PubMed=12504025; DOI=10.1016/S1097-2765(02)00783-9;
RA Liu J., Furukawa M., Matsumoto T., Xiong Y.;
RT "NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of
RT CUL1-SKP1 binding and SCF ligases.";
RL Mol. Cell 10:1511-1518(2002).
RN [12]
RP FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B AND RBX1,
RP AND MASS SPECTROMETRY.
RX PubMed=12609982; DOI=10.1074/jbc.M213070200;
RA Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.;
RT "TIP120A associates with cullins and modulates ubiquitin ligase
RT activity.";
RL J. Biol. Chem. 278:15905-15910(2003).
RN [13]
RP FUNCTION, AND INTERACTION WITH CUL3.
RX PubMed=16449638; DOI=10.1128/MCB.26.4.1235-1244.2006;
RA Lo S.C., Hannink M.;
RT "CAND1-mediated substrate adaptor recycling is required for efficient
RT repression of Nrf2 by Keap1.";
RL Mol. Cell. Biol. 26:1235-1244(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-971, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP INDUCTION.
RX PubMed=20820187; DOI=10.1038/pcan.2010.32;
RA Murata T., Takayama K., Katayama S., Urano T., Horie-Inoue K.,
RA Ikeda K., Takahashi S., Kawazu C., Hasegawa A., Ouchi Y., Homma Y.,
RA Hayashizaki Y., Inoue S.;
RT "miR-148a is an androgen-responsive microRNA that promotes LNCaP
RT prostate cell growth by repressing its target CAND1 expression.";
RL Prostate Cancer Prostatic Dis. 13:356-361(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP INTERACTION WITH CUL2.
RX PubMed=21778237; DOI=10.1074/jbc.M111.278408;
RA Mao X., Gluck N., Chen B., Starokadomskyy P., Li H., Maine G.N.,
RA Burstein E.;
RT "COMMD1 (copper metabolism MURR1 domain-containing protein 1)
RT regulates Cullin RING ligases by preventing CAND1 (Cullin-associated
RT Nedd8-dissociated protein 1) binding.";
RL J. Biol. Chem. 286:32355-32365(2011).
RN [21]
RP FUNCTION, INTERACTION WITH CUL2; CUL3; CUL4A AND CUL5, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21249194; DOI=10.1371/journal.pone.0016071;
RA Chua Y.S., Boh B.K., Ponyeam W., Hagen T.;
RT "Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo.";
RL PLoS ONE 6:E16071-E16071(2011).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP FUNCTION, AND REACTION MECHANISM.
RX PubMed=23453757; DOI=10.1016/j.cell.2013.02.024;
RA Pierce N.W., Lee J.E., Liu X., Sweredoski M.J., Graham R.L.,
RA Larimore E.A., Rome M., Zheng N., Clurman B.E., Hess S., Shan S.O.,
RA Deshaies R.J.;
RT "Cand1 promotes assembly of new SCF complexes through dynamic exchange
RT of F box proteins.";
RL Cell 153:206-215(2013).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CUL1 AND RBX1.
RX PubMed=15537541; DOI=10.1016/j.cell.2004.10.019;
RA Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J.,
RA Xiong Y., Zheng N.;
RT "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory
RT mechanisms for the assembly of the multisubunit cullin-dependent
RT ubiquitin ligases.";
RL Cell 119:517-528(2004).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEX WITH CUL4B AND RBX1.
RX PubMed=22118460; DOI=10.1016/j.cell.2011.10.035;
RA Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M.,
RA Faty M., Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S.,
RA Gut H., Sugasawa K., Thoma N.H.;
RT "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture,
RT targeting, and activation.";
RL Cell 147:1024-1039(2011).
CC -!- FUNCTION: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3
CC ubiquitin ligase complexes that promotes the exchange of the
CC substrate-recognition F-box subunit in SCF complexes, thereby
CC playing a key role in the cellular repertoire of SCF complexes.
CC Acts as a F-box protein exchange factor. The exchange activity of
CC CAND1 is coupled with cycles of neddylation conjugation: in the
CC deneddylated state, cullin-binding CAND1 binds CUL1-RBX1,
CC increasing dissociation of the SCF complex and promoting exchange
CC of the F-box protein. Probably plays a similar role in other
CC cullin-RING E3 ubiquitin ligase complexes.
CC -!- SUBUNIT: Interacts with TBP (By similarity). Part of a complex
CC that contains CUL1 and RBX1. Interacts with unneddylated cullins:
CC interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5. Does not
CC bind neddylated CUL1. Interaction with cullins is abolished in
CC presence of COMMD1, which antagonizes with CAND1 for interacting
CC with cullins.
CC -!- INTERACTION:
CC Q13616:CUL1; NbExp=19; IntAct=EBI-456077, EBI-359390;
CC Q13617:CUL2; NbExp=3; IntAct=EBI-456077, EBI-456179;
CC Q13618:CUL3; NbExp=2; IntAct=EBI-456077, EBI-456129;
CC Q13619:CUL4A; NbExp=3; IntAct=EBI-456077, EBI-456106;
CC Q13620:CUL4B; NbExp=3; IntAct=EBI-456077, EBI-456067;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86VP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VP6-2; Sequence=VSP_013948;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q86VP6-3; Sequence=VSP_013947, VSP_013949, VSP_013950;
CC Note=No experimental confirmation available;
CC -!- INDUCTION: Repressed by miR-148a.
CC -!- MISCELLANEOUS: A model has been proposed to explain the mechanisms
CC of cullin-RING E3 ubiquitin ligase complexes assembly. According
CC to this hypothesis, cullin-RING E3 ubiquitin ligase complexes
CC exist in a 'stable' active state when saturated with substrate,
CC occluding access to deneddylation by the COP9 signalosome (CSN)
CC complex. The neddylation-conjugated cullin-RING E3 ubiquitin
CC ligase complexes mediate ubiquitination of substrates and can
CC recruit downstream factors involved in substrate degradation.
CC Depletion of the substrate promotes the ability of CSN to bind the
CC cullin-RING E3 ubiquitin ligase complex and mediate deneddylation.
CC In this 'intermediate' deneddylated state, the complex can bind
CC CAND1 and enter the 'exchange' state, resulting in high increase
CC in dissociation rate of the substrate-recognition subunit. The
CC resulting CAND1-cullin-RING complex rapidly assembles with another
CC available substrate-recognition subunit to form an unstable
CC ternary intermediate and yield a new cullin-RING E3 ubiquitin
CC ligase complex. Subsequent neddylation of the cullin, which is
CC stabilized by substrate, completes the cycle (PubMed:23453757).
CC -!- SIMILARITY: Belongs to the CAND family.
CC -!- SIMILARITY: Contains 27 HEAT repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74852.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB55090.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
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DR EMBL; AB020636; BAA74852.2; ALT_INIT; mRNA.
DR EMBL; AF157326; AAF67492.1; -; mRNA.
DR EMBL; AL133560; CAB63714.1; -; mRNA.
DR EMBL; AL136810; CAB66744.1; -; mRNA.
DR EMBL; AL833880; CAD38737.1; -; mRNA.
DR EMBL; CH471054; EAW97172.1; -; Genomic_DNA.
DR EMBL; BC004232; AAH04232.1; -; mRNA.
DR EMBL; BC026220; AAH26220.1; -; mRNA.
DR EMBL; BC050341; AAH50341.1; -; mRNA.
DR EMBL; AK027404; BAB55090.1; ALT_INIT; mRNA.
DR EMBL; AK027783; BAB55365.1; -; mRNA.
DR EMBL; AK314358; BAG36990.1; -; mRNA.
DR PIR; T43441; T43441.
DR RefSeq; NP_060918.2; NM_018448.3.
DR UniGene; Hs.546407; -.
DR PDB; 1U6G; X-ray; 3.10 A; C=1-1230.
DR PDB; 4A0C; X-ray; 3.80 A; A/B=1-1230.
DR PDBsum; 1U6G; -.
DR PDBsum; 4A0C; -.
DR ProteinModelPortal; Q86VP6; -.
DR DIP; DIP-31608N; -.
DR IntAct; Q86VP6; 15.
DR MINT; MINT-4999459; -.
DR PhosphoSite; Q86VP6; -.
DR DMDM; 67460541; -.
DR PaxDb; Q86VP6; -.
DR PRIDE; Q86VP6; -.
DR DNASU; 55832; -.
DR Ensembl; ENST00000544619; ENSP00000444089; ENSG00000111530.
DR Ensembl; ENST00000545606; ENSP00000442318; ENSG00000111530.
DR GeneID; 55832; -.
DR KEGG; hsa:55832; -.
DR UCSC; uc001stn.2; human.
DR CTD; 55832; -.
DR GeneCards; GC12P067663; -.
DR HGNC; HGNC:30688; CAND1.
DR MIM; 607727; gene.
DR neXtProt; NX_Q86VP6; -.
DR PharmGKB; PA142672207; -.
DR eggNOG; NOG278162; -.
DR HOVERGEN; HBG053467; -.
DR InParanoid; Q86VP6; -.
DR KO; K17263; -.
DR OMA; AIACMGQ; -.
DR OrthoDB; EOG77HDCZ; -.
DR PhylomeDB; Q86VP6; -.
DR ChiTaRS; CAND1; human.
DR EvolutionaryTrace; Q86VP6; -.
DR GeneWiki; CAND1; -.
DR GenomeRNAi; 55832; -.
DR NextBio; 61049; -.
DR PRO; PR:Q86VP6; -.
DR ArrayExpress; Q86VP6; -.
DR Bgee; Q86VP6; -.
DR Genevestigator; Q86VP6; -.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0010265; P:SCF complex assembly; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013932; TATA-bd_TIP120.
DR Pfam; PF08623; TIP120; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1230 Cullin-associated NEDD8-dissociated
FT protein 1.
FT /FTId=PRO_0000089293.
FT REPEAT 2 39 HEAT 1.
FT REPEAT 44 81 HEAT 2.
FT REPEAT 83 119 HEAT 3.
FT REPEAT 131 165 HEAT 4.
FT REPEAT 171 208 HEAT 5.
FT REPEAT 210 247 HEAT 6.
FT REPEAT 248 282 HEAT 7.
FT REPEAT 289 366 HEAT 8.
FT REPEAT 370 407 HEAT 9.
FT REPEAT 424 467 HEAT 10.
FT REPEAT 471 510 HEAT 11.
FT REPEAT 515 552 HEAT 12.
FT REPEAT 563 602 HEAT 13.
FT REPEAT 606 643 HEAT 14.
FT REPEAT 646 683 HEAT 15.
FT REPEAT 688 725 HEAT 16.
FT REPEAT 729 768 HEAT 17.
FT REPEAT 770 808 HEAT 18.
FT REPEAT 809 845 HEAT 19.
FT REPEAT 852 889 HEAT 20.
FT REPEAT 890 927 HEAT 21.
FT REPEAT 928 960 HEAT 22.
FT REPEAT 961 998 HEAT 23.
FT REPEAT 1002 1039 HEAT 24.
FT REPEAT 1043 1097 HEAT 25.
FT REPEAT 1099 1133 HEAT 26.
FT REPEAT 1140 1189 HEAT 27.
FT COMPBIAS 314 344 Asp-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 55 55 N6-acetyllysine.
FT MOD_RES 335 335 Phosphoserine.
FT MOD_RES 971 971 N6-acetyllysine.
FT VAR_SEQ 1 157 Missing (in isoform 3).
FT /FTId=VSP_013947.
FT VAR_SEQ 458 625 Missing (in isoform 2).
FT /FTId=VSP_013948.
FT VAR_SEQ 549 560 VIRPLDQPSSFD -> AHHMPEAQWLRL (in isoform
FT 3).
FT /FTId=VSP_013949.
FT VAR_SEQ 561 1230 Missing (in isoform 3).
FT /FTId=VSP_013950.
FT VARIANT 803 803 V -> A (in dbSNP:rs12580996).
FT /FTId=VAR_054041.
FT VARIANT 952 952 A -> V (in dbSNP:rs17854618).
FT /FTId=VAR_025327.
FT CONFLICT 272 272 R -> K (in Ref. 7; BAB55365).
FT CONFLICT 457 457 M -> I (in Ref. 7; BAB55090).
FT CONFLICT 606 606 S -> P (in Ref. 3; AAF67492).
FT CONFLICT 609 609 P -> S (in Ref. 3; AAF67492).
FT CONFLICT 1047 1047 T -> S (in Ref. 3; AAF67492).
FT CONFLICT 1177 1177 M -> T (in Ref. 7; BAB55090).
FT HELIX 6 14
FT HELIX 20 33
FT STRAND 35 37
FT HELIX 45 56
FT HELIX 62 76
FT HELIX 81 94
FT STRAND 98 100
FT HELIX 101 116
FT HELIX 127 142
FT HELIX 148 164
FT TURN 170 172
FT HELIX 173 180
FT HELIX 181 185
FT HELIX 189 202
FT TURN 203 205
FT HELIX 214 224
FT HELIX 234 244
FT HELIX 247 249
FT HELIX 256 264
FT TURN 269 271
FT HELIX 272 284
FT HELIX 291 301
FT HELIX 348 361
FT HELIX 368 372
FT TURN 373 375
FT HELIX 376 380
FT STRAND 386 388
FT HELIX 389 405
FT HELIX 424 431
FT HELIX 434 442
FT HELIX 448 464
FT TURN 466 469
FT HELIX 470 472
FT HELIX 473 483
FT STRAND 487 489
FT HELIX 491 506
FT HELIX 510 513
FT HELIX 514 517
FT TURN 518 520
FT HELIX 521 528
FT HELIX 533 550
FT STRAND 553 555
FT HELIX 562 576
FT STRAND 579 581
FT HELIX 583 599
FT HELIX 601 603
FT HELIX 607 618
FT STRAND 621 623
FT HELIX 624 635
FT HELIX 645 658
FT HELIX 664 680
FT HELIX 687 694
FT HELIX 698 700
FT HELIX 706 719
FT HELIX 724 729
FT TURN 730 734
FT HELIX 735 742
FT HELIX 749 763
FT HELIX 772 779
FT TURN 781 785
FT HELIX 793 809
FT HELIX 815 818
FT TURN 819 824
FT TURN 826 829
FT HELIX 832 848
FT HELIX 856 863
FT HELIX 864 866
FT HELIX 870 886
FT HELIX 888 900
FT HELIX 903 905
FT HELIX 906 918
FT TURN 923 925
FT HELIX 926 936
FT HELIX 947 960
FT HELIX 963 965
FT HELIX 967 970
FT TURN 971 973
FT STRAND 974 977
FT HELIX 979 988
FT HELIX 990 992
FT HELIX 1001 1007
FT TURN 1009 1014
FT STRAND 1015 1019
FT HELIX 1021 1036
FT HELIX 1038 1040
FT HELIX 1042 1044
FT HELIX 1045 1054
FT HELIX 1060 1062
FT STRAND 1063 1068
FT STRAND 1071 1076
FT HELIX 1079 1094
FT STRAND 1098 1100
FT HELIX 1102 1111
FT HELIX 1117 1132
FT HELIX 1136 1139
FT TURN 1140 1145
FT HELIX 1146 1154
FT HELIX 1163 1182
FT STRAND 1190 1194
FT HELIX 1200 1208
SQ SEQUENCE 1230 AA; 136376 MW; FE344558F72D79D8 CRC64;
MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILKLLEDK
NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE QLRDISSIGL KTVIGELPPA
SSGSALAANV CKKITGRLTS AIAKQEDVSV QLEALDIMAD MLSRQGGLLV NFHPSILTCL
LPQLTSPRLA VRKRTIIALG HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA
ISRQAGHRIG EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI
CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR RAAAKCLDAV
VSTRHEMLPE FYKTVSPALI SRFKEREENV KADVFHAYLS LLKQTRPVQS WLCDPDAMEQ
GETPLTMLQS QVPNIVKALH KQMKEKSVKT RQCCFNMLTE LVNVLPGALT QHIPVLVPGI
IFSLNDKSSS SNLKIDALSC LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL
LVTQQLVKVI RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL
GDNLGSDLPN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE GVPILASFLR
KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL ISESDMHVSQ MAISFLTTLA
KVYPSSLSKI SGSILNELIG LVRSPLLQGG ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT
GPVYSQSTAL THKQSYYSIA KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL
SLGEVGHHID LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT
SQPKRQYLLL HSLKEIISSA SVVGLKPYVE NIWALLLKHC ECAEEGTRNV VAECLGKLTL
IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI DPLLKNCIGD FLKTLEDPDL
NVRRVALVTF NSAAHNKPSL IRDLLDTVLP HLYNETKVRK ELIREVEMGP FKHTVDDGLD
IRKAAFECMY TLLDSCLDRL DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ
RLDRLVEPLR ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS
QISSNPELAA IFESIQKDSS STNLESMDTS
//
MIM
607727
*RECORD*
*FIELD* NO
607727
*FIELD* TI
*607727 CULLIN-ASSOCIATED NEDDYLATION-DISSOCIATED PROTEIN 1; CAND1
;;TBP-INTERACTING PROTEIN, 120-KD, A;;
read moreTIP120A;;
TIP120;;
p120(CAND1);;
KIAA0829
*FIELD* TX
CLONING
Using histidine-tagged TATA-binding protein (TBP; 600075) as a ligand
for affinity-purification of TBP-interacting proteins, Yogosawa et al.
(1996) purified a 120-kD protein, which they termed Tip120, from rat
liver nuclear extracts. They obtained a full-length cDNA encoding Tip120
by screening a rat liver cDNA library. The rat Tip120 protein contains
1,230 amino acids and has a calculated molecular mass of 135 kD.
Northern blot analysis detected a 4.5-kb transcript.
GENE FUNCTION
Yogosawa et al. (1996) showed that recombinant rat Tip120 interacted
directly with TBP under a physiologic condition in vitro.
Immunoprecipitation analysis indicated that Tip120 associated with TBP
in nuclear extracts.
Zheng et al. (2002) isolated TIP120A as a cullin-1 (CUL1;
603134)-binding protein that they designated CAND1. They determined that
the majority of CUL1 is in a complex with CAND1 and ROC1 (603814)
independent of SKP1 (601434) and the F box protein SKP2 (601436). Both
in vivo and in vitro, CAND1 prevented binding of SKP1 and SKP2 to CUL1,
while dissociation of CAND1 from CUL1 promoted the reverse reaction.
Neddylation of CUL1 or the presence of SKP1 and ATP caused CAND1
dissociation. These data suggested that CAND1 regulates the formation of
the SCF (SKP1, CUL1/Cdc53, F box protein) complex and that its
dissociation from CUL1 is coupled with the incorporation of F box
proteins into the SCF complex, causing their destabilization.
Liu et al. (2002) showed that p120(CAND1) selectively binds to
unneddylated CUL1 and is dissociated by CUL1 neddylation. CAND1 formed a
ternary complex with CUL1 and ROC1. It dissociated SKP1 from CUL1 and
inhibited SCF ligase activity in vitro. Suppression of CAND1 in vivo
increased the level of the CUL1-SKP1 complex. The authors concluded
that, by restricting SKP1-CUL1 interaction, CAND1 regulates the assembly
of productive SCF ubiquitin ligases, allowing a common CUL1-ROC core to
be utilized by a large number of SKP1-F box-substrate subcomplexes.
MAPPING
By FISH, Yogosawa et al. (1999) mapped the CAND1 gene to chromosome
12q14.
*FIELD* RF
1. Liu, J.; Furukawa, M.; Matsumoto, T.; Xiong, Y.: NEDD8 modification
of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding
and SCF ligases. Molec. Cell 10: 1511-1518, 2002.
2. Yogosawa, S.; Kayukawa, K.; Kawata, T.; Makino, Y.; Inoue, S.;
Okuda, A.; Muramatsu, M.; Tamura, T.: Induced expression, localization,
and chromosome mapping of a gene for the TBP-interacting protein 120A. Biochem.
Biophys. Res. Commun. 266: 123-128, 1999.
3. Yogosawa, S.; Makino, Y.; Yoshida, T.; Kishimoto, T.; Muramatsu,
M.; Tamura, T.: Molecular cloning of a novel 120-kDa TBP-interacting
protein. Biochem. Biophys. Res. Commun. 229: 612-617, 1996.
4. Zheng, J.; Yang, X.; Harrell, J. M.; Ryzhikov, S.; Shim, E.-H.;
Lykke-Andersen, K.; Wei, N.; Sun, H.; Kobayashi, R.; Zhang, H.: CAND1
binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin
E3 ligase complex. Molec. Cell 10: 1519-1526, 2002.
*FIELD* CN
Patricia A. Hartz - updated: 8/29/2006
*FIELD* CD
Stylianos E. Antonarakis: 4/28/2003
*FIELD* ED
wwang: 09/13/2006
wwang: 9/13/2006
terry: 8/29/2006
mgross: 4/28/2003
*RECORD*
*FIELD* NO
607727
*FIELD* TI
*607727 CULLIN-ASSOCIATED NEDDYLATION-DISSOCIATED PROTEIN 1; CAND1
;;TBP-INTERACTING PROTEIN, 120-KD, A;;
read moreTIP120A;;
TIP120;;
p120(CAND1);;
KIAA0829
*FIELD* TX
CLONING
Using histidine-tagged TATA-binding protein (TBP; 600075) as a ligand
for affinity-purification of TBP-interacting proteins, Yogosawa et al.
(1996) purified a 120-kD protein, which they termed Tip120, from rat
liver nuclear extracts. They obtained a full-length cDNA encoding Tip120
by screening a rat liver cDNA library. The rat Tip120 protein contains
1,230 amino acids and has a calculated molecular mass of 135 kD.
Northern blot analysis detected a 4.5-kb transcript.
GENE FUNCTION
Yogosawa et al. (1996) showed that recombinant rat Tip120 interacted
directly with TBP under a physiologic condition in vitro.
Immunoprecipitation analysis indicated that Tip120 associated with TBP
in nuclear extracts.
Zheng et al. (2002) isolated TIP120A as a cullin-1 (CUL1;
603134)-binding protein that they designated CAND1. They determined that
the majority of CUL1 is in a complex with CAND1 and ROC1 (603814)
independent of SKP1 (601434) and the F box protein SKP2 (601436). Both
in vivo and in vitro, CAND1 prevented binding of SKP1 and SKP2 to CUL1,
while dissociation of CAND1 from CUL1 promoted the reverse reaction.
Neddylation of CUL1 or the presence of SKP1 and ATP caused CAND1
dissociation. These data suggested that CAND1 regulates the formation of
the SCF (SKP1, CUL1/Cdc53, F box protein) complex and that its
dissociation from CUL1 is coupled with the incorporation of F box
proteins into the SCF complex, causing their destabilization.
Liu et al. (2002) showed that p120(CAND1) selectively binds to
unneddylated CUL1 and is dissociated by CUL1 neddylation. CAND1 formed a
ternary complex with CUL1 and ROC1. It dissociated SKP1 from CUL1 and
inhibited SCF ligase activity in vitro. Suppression of CAND1 in vivo
increased the level of the CUL1-SKP1 complex. The authors concluded
that, by restricting SKP1-CUL1 interaction, CAND1 regulates the assembly
of productive SCF ubiquitin ligases, allowing a common CUL1-ROC core to
be utilized by a large number of SKP1-F box-substrate subcomplexes.
MAPPING
By FISH, Yogosawa et al. (1999) mapped the CAND1 gene to chromosome
12q14.
*FIELD* RF
1. Liu, J.; Furukawa, M.; Matsumoto, T.; Xiong, Y.: NEDD8 modification
of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding
and SCF ligases. Molec. Cell 10: 1511-1518, 2002.
2. Yogosawa, S.; Kayukawa, K.; Kawata, T.; Makino, Y.; Inoue, S.;
Okuda, A.; Muramatsu, M.; Tamura, T.: Induced expression, localization,
and chromosome mapping of a gene for the TBP-interacting protein 120A. Biochem.
Biophys. Res. Commun. 266: 123-128, 1999.
3. Yogosawa, S.; Makino, Y.; Yoshida, T.; Kishimoto, T.; Muramatsu,
M.; Tamura, T.: Molecular cloning of a novel 120-kDa TBP-interacting
protein. Biochem. Biophys. Res. Commun. 229: 612-617, 1996.
4. Zheng, J.; Yang, X.; Harrell, J. M.; Ryzhikov, S.; Shim, E.-H.;
Lykke-Andersen, K.; Wei, N.; Sun, H.; Kobayashi, R.; Zhang, H.: CAND1
binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin
E3 ligase complex. Molec. Cell 10: 1519-1526, 2002.
*FIELD* CN
Patricia A. Hartz - updated: 8/29/2006
*FIELD* CD
Stylianos E. Antonarakis: 4/28/2003
*FIELD* ED
wwang: 09/13/2006
wwang: 9/13/2006
terry: 8/29/2006
mgross: 4/28/2003