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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)

 CAND1_HUMAN             Reviewed;        1230 AA.
Q86VP6; B2RAU3; O94918; Q6PIY4; Q8NDJ4; Q96JZ9; Q96T19; Q9BTC4;
Q9H0G2; Q9P0H7; Q9UF85;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
30-AUG-2017, entry version 150.
RecName: Full=Cullin-associated NEDD8-dissociated protein 1;
AltName: Full=Cullin-associated and neddylation-dissociated protein 1;
AltName: Full=TBP-interacting protein of 120 kDa A;
Short=TBP-interacting protein 120A;
AltName: Full=p120 CAND1;
Name=CAND1; Synonyms=KIAA0829, TIP120, TIP120A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[2]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-952.
TISSUE=Cervix, Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
PROTEIN SEQUENCE OF 2-14 AND 374-382, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Ramsay A., Leung H.Y.;
Submitted (MAR-2009) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 2-14; 535-548; 668-679; 730-743; 859-873; 958-969
AND 983-990, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[10]
PARTIAL PROTEIN SEQUENCE, FUNCTION, AND IDENTIFICATION IN A COMPLEX
WITH CUL1 AND RBX1.
PubMed=12504026; DOI=10.1016/S1097-2765(02)00784-0;
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.";
Mol. Cell 10:1519-1526(2002).
[11]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1 AND RBX1, AND
INTERACTION WITH UNNEDDYLATED CUL1; CUL4A AND CUL5.
PubMed=12504025; DOI=10.1016/S1097-2765(02)00783-9;
Liu J., Furukawa M., Matsumoto T., Xiong Y.;
"NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of
CUL1-SKP1 binding and SCF ligases.";
Mol. Cell 10:1511-1518(2002).
[12]
FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B AND RBX1,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12609982; DOI=10.1074/jbc.M213070200;
Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.;
"TIP120A associates with cullins and modulates ubiquitin ligase
activity.";
J. Biol. Chem. 278:15905-15910(2003).
[13]
FUNCTION, AND INTERACTION WITH CUL3.
PubMed=16449638; DOI=10.1128/MCB.26.4.1235-1244.2006;
Lo S.C., Hannink M.;
"CAND1-mediated substrate adaptor recycling is required for efficient
repression of Nrf2 by Keap1.";
Mol. Cell. Biol. 26:1235-1244(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-971, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
INDUCTION.
PubMed=20820187; DOI=10.1038/pcan.2010.32;
Murata T., Takayama K., Katayama S., Urano T., Horie-Inoue K.,
Ikeda K., Takahashi S., Kawazu C., Hasegawa A., Ouchi Y., Homma Y.,
Hayashizaki Y., Inoue S.;
"miR-148a is an androgen-responsive microRNA that promotes LNCaP
prostate cell growth by repressing its target CAND1 expression.";
Prostate Cancer Prostatic Dis. 13:356-361(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
INTERACTION WITH CUL2.
PubMed=21778237; DOI=10.1074/jbc.M111.278408;
Mao X., Gluck N., Chen B., Starokadomskyy P., Li H., Maine G.N.,
Burstein E.;
"COMMD1 (copper metabolism MURR1 domain-containing protein 1)
regulates Cullin RING ligases by preventing CAND1 (Cullin-associated
Nedd8-dissociated protein 1) binding.";
J. Biol. Chem. 286:32355-32365(2011).
[21]
FUNCTION, INTERACTION WITH CUL2; CUL3; CUL4A AND CUL5, AND SUBCELLULAR
LOCATION.
PubMed=21249194; DOI=10.1371/journal.pone.0016071;
Chua Y.S., Boh B.K., Ponyeam W., Hagen T.;
"Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo.";
PLoS ONE 6:E16071-E16071(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
FUNCTION, AND REACTION MECHANISM.
PubMed=23453757; DOI=10.1016/j.cell.2013.02.024;
Pierce N.W., Lee J.E., Liu X., Sweredoski M.J., Graham R.L.,
Larimore E.A., Rome M., Zheng N., Clurman B.E., Hess S., Shan S.O.,
Deshaies R.J.;
"Cand1 promotes assembly of new SCF complexes through dynamic exchange
of F box proteins.";
Cell 153:206-215(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
INTERACTION WITH DCUN1D3.
PubMed=25349211; DOI=10.1074/jbc.M114.585505;
Huang G., Stock C., Bommelje C.C., Weeda V.B., Shah K., Bains S.,
Buss E., Shaha M., Rechler W., Ramanathan S.Y., Singh B.;
"SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity
of SCCRO (DCUN1D1).";
J. Biol. Chem. 289:34728-34742(2014).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CUL1 AND RBX1.
PubMed=15537541; DOI=10.1016/j.cell.2004.10.019;
Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J.,
Xiong Y., Zheng N.;
"Structure of the Cand1-Cul1-Roc1 complex reveals regulatory
mechanisms for the assembly of the multisubunit cullin-dependent
ubiquitin ligases.";
Cell 119:517-528(2004).
[30]
X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEX WITH CUL4B AND RBX1.
PubMed=22118460; DOI=10.1016/j.cell.2011.10.035;
Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M.,
Faty M., Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S.,
Gut H., Sugasawa K., Thoma N.H.;
"The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture,
targeting, and activation.";
Cell 147:1024-1039(2011).
-!- FUNCTION: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3
ubiquitin ligase complexes that promotes the exchange of the
substrate-recognition F-box subunit in SCF complexes, thereby
playing a key role in the cellular repertoire of SCF complexes.
Acts as a F-box protein exchange factor. The exchange activity of
CAND1 is coupled with cycles of neddylation conjugation: in the
deneddylated state, cullin-binding CAND1 binds CUL1-RBX1,
increasing dissociation of the SCF complex and promoting exchange
of the F-box protein. Probably plays a similar role in other
cullin-RING E3 ubiquitin ligase complexes.
{ECO:0000269|PubMed:12504025, ECO:0000269|PubMed:12504026,
ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:16449638,
ECO:0000269|PubMed:21249194, ECO:0000269|PubMed:23453757}.
-!- SUBUNIT: Interacts with TBP (By similarity). Part of a complex
that contains CUL1 and RBX1. Interacts with unneddylated cullins:
interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5. Does not
bind neddylated CUL1. Interaction with cullins is abolished in
presence of COMMD1, which antagonizes with CAND1 for interacting
with cullins. Interacts with DCUN1D3. {ECO:0000250,
ECO:0000269|PubMed:12504025, ECO:0000269|PubMed:12504026,
ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:15537541,
ECO:0000269|PubMed:16449638, ECO:0000269|PubMed:21249194,
ECO:0000269|PubMed:21778237, ECO:0000269|PubMed:22118460,
ECO:0000269|PubMed:25349211}.
-!- INTERACTION:
Q13616:CUL1; NbExp=19; IntAct=EBI-456077, EBI-359390;
Q13617:CUL2; NbExp=3; IntAct=EBI-456077, EBI-456179;
Q13618:CUL3; NbExp=2; IntAct=EBI-456077, EBI-456129;
Q13619:CUL4A; NbExp=3; IntAct=EBI-456077, EBI-456106;
Q13620:CUL4B; NbExp=4; IntAct=EBI-456077, EBI-456067;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21249194}.
Nucleus {ECO:0000269|PubMed:21249194}. Note=Predominantly
cytoplasmic.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q86VP6-1; Sequence=Displayed;
Name=2;
IsoId=Q86VP6-2; Sequence=VSP_013948;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q86VP6-3; Sequence=VSP_013947, VSP_013949, VSP_013950;
Note=No experimental confirmation available.;
-!- INDUCTION: Repressed by miR-148a. {ECO:0000269|PubMed:20820187}.
-!- MISCELLANEOUS: A model has been proposed to explain the mechanisms
of cullin-RING E3 ubiquitin ligase complexes assembly. According
to this hypothesis, cullin-RING E3 ubiquitin ligase complexes
exist in a 'stable' active state when saturated with substrate,
occluding access to deneddylation by the COP9 signalosome (CSN)
complex. The neddylation-conjugated cullin-RING E3 ubiquitin
ligase complexes mediate ubiquitination of substrates and can
recruit downstream factors involved in substrate degradation.
Depletion of the substrate promotes the ability of CSN to bind the
cullin-RING E3 ubiquitin ligase complex and mediate deneddylation.
In this 'intermediate' deneddylated state, the complex can bind
CAND1 and enter the 'exchange' state, resulting in high increase
in dissociation rate of the substrate-recognition subunit. The
resulting CAND1-cullin-RING complex rapidly assembles with another
available substrate-recognition subunit to form an unstable
ternary intermediate and yield a new cullin-RING E3 ubiquitin
ligase complex. Subsequent neddylation of the cullin, which is
stabilized by substrate, completes the cycle (PubMed:23453757).
{ECO:0000305|PubMed:23453757}.
-!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA74852.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB55090.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB020636; BAA74852.2; ALT_INIT; mRNA.
EMBL; AF157326; AAF67492.1; -; mRNA.
EMBL; AL133560; CAB63714.1; -; mRNA.
EMBL; AL136810; CAB66744.1; -; mRNA.
EMBL; AL833880; CAD38737.1; -; mRNA.
EMBL; CH471054; EAW97172.1; -; Genomic_DNA.
EMBL; BC004232; AAH04232.1; -; mRNA.
EMBL; BC026220; AAH26220.1; -; mRNA.
EMBL; BC050341; AAH50341.1; -; mRNA.
EMBL; AK027404; BAB55090.1; ALT_INIT; mRNA.
EMBL; AK027783; BAB55365.1; -; mRNA.
EMBL; AK314358; BAG36990.1; -; mRNA.
CCDS; CCDS8977.1; -. [Q86VP6-1]
PIR; T43441; T43441.
RefSeq; NP_060918.2; NM_018448.4. [Q86VP6-1]
UniGene; Hs.546407; -.
PDB; 1U6G; X-ray; 3.10 A; C=1-1230.
PDB; 4A0C; X-ray; 3.80 A; A/B=1-1230.
PDBsum; 1U6G; -.
PDBsum; 4A0C; -.
ProteinModelPortal; Q86VP6; -.
SMR; Q86VP6; -.
BioGrid; 120937; 704.
DIP; DIP-31608N; -.
IntAct; Q86VP6; 31.
MINT; MINT-4999459; -.
STRING; 9606.ENSP00000299218; -.
iPTMnet; Q86VP6; -.
PhosphoSitePlus; Q86VP6; -.
SwissPalm; Q86VP6; -.
BioMuta; CAND1; -.
DMDM; 67460541; -.
EPD; Q86VP6; -.
MaxQB; Q86VP6; -.
PaxDb; Q86VP6; -.
PeptideAtlas; Q86VP6; -.
PRIDE; Q86VP6; -.
DNASU; 55832; -.
Ensembl; ENST00000545606; ENSP00000442318; ENSG00000111530. [Q86VP6-1]
GeneID; 55832; -.
KEGG; hsa:55832; -.
UCSC; uc001stn.3; human. [Q86VP6-1]
CTD; 55832; -.
DisGeNET; 55832; -.
GeneCards; CAND1; -.
HGNC; HGNC:30688; CAND1.
HPA; HPA055748; -.
HPA; HPA062833; -.
HPA; HPA069053; -.
MIM; 607727; gene.
neXtProt; NX_Q86VP6; -.
OpenTargets; ENSG00000111530; -.
PharmGKB; PA142672207; -.
eggNOG; KOG1824; Eukaryota.
eggNOG; ENOG410XPK4; LUCA.
GeneTree; ENSGT00390000017740; -.
HOVERGEN; HBG053467; -.
InParanoid; Q86VP6; -.
KO; K17263; -.
OMA; MASHQYH; -.
OrthoDB; EOG091G017Q; -.
PhylomeDB; Q86VP6; -.
TreeFam; TF300355; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-917937; Iron uptake and transport.
ChiTaRS; CAND1; human.
EvolutionaryTrace; Q86VP6; -.
GeneWiki; CAND1; -.
GenomeRNAi; 55832; -.
PRO; PR:Q86VP6; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111530; -.
ExpressionAtlas; Q86VP6; baseline and differential.
Genevisible; Q86VP6; HS.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0017025; F:TBP-class protein binding; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0010265; P:SCF complex assembly; IDA:UniProtKB.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR013932; TATA-bd_TIP120.
Pfam; PF08623; TIP120; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.8, ECO:0000269|Ref.9}.
CHAIN 2 1230 Cullin-associated NEDD8-dissociated
protein 1.
/FTId=PRO_0000089293.
REPEAT 2 39 HEAT 1.
REPEAT 44 81 HEAT 2.
REPEAT 83 119 HEAT 3.
REPEAT 131 165 HEAT 4.
REPEAT 171 208 HEAT 5.
REPEAT 210 247 HEAT 6.
REPEAT 248 282 HEAT 7.
REPEAT 289 366 HEAT 8.
REPEAT 370 407 HEAT 9.
REPEAT 424 467 HEAT 10.
REPEAT 471 510 HEAT 11.
REPEAT 515 552 HEAT 12.
REPEAT 563 602 HEAT 13.
REPEAT 606 643 HEAT 14.
REPEAT 646 683 HEAT 15.
REPEAT 688 725 HEAT 16.
REPEAT 729 768 HEAT 17.
REPEAT 770 808 HEAT 18.
REPEAT 809 845 HEAT 19.
REPEAT 852 889 HEAT 20.
REPEAT 890 927 HEAT 21.
REPEAT 928 960 HEAT 22.
REPEAT 961 998 HEAT 23.
REPEAT 1002 1039 HEAT 24.
REPEAT 1043 1097 HEAT 25.
REPEAT 1099 1133 HEAT 26.
REPEAT 1140 1189 HEAT 27.
COMPBIAS 314 344 Asp-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.8, ECO:0000269|Ref.9}.
MOD_RES 55 55 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 971 971 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 157 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_013947.
VAR_SEQ 458 625 Missing (in isoform 2).
{ECO:0000303|PubMed:11230166}.
/FTId=VSP_013948.
VAR_SEQ 549 560 VIRPLDQPSSFD -> AHHMPEAQWLRL (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_013949.
VAR_SEQ 561 1230 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_013950.
VARIANT 803 803 V -> A (in dbSNP:rs12580996).
/FTId=VAR_054041.
VARIANT 952 952 A -> V (in dbSNP:rs17854618).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_025327.
CONFLICT 272 272 R -> K (in Ref. 7; BAB55365).
{ECO:0000305}.
CONFLICT 457 457 M -> I (in Ref. 7; BAB55090).
{ECO:0000305}.
CONFLICT 606 606 S -> P (in Ref. 3; AAF67492).
{ECO:0000305}.
CONFLICT 609 609 P -> S (in Ref. 3; AAF67492).
{ECO:0000305}.
CONFLICT 1047 1047 T -> S (in Ref. 3; AAF67492).
{ECO:0000305}.
CONFLICT 1177 1177 M -> T (in Ref. 7; BAB55090).
{ECO:0000305}.
HELIX 6 14 {ECO:0000244|PDB:1U6G}.
HELIX 20 33 {ECO:0000244|PDB:1U6G}.
STRAND 35 37 {ECO:0000244|PDB:1U6G}.
HELIX 45 56 {ECO:0000244|PDB:1U6G}.
HELIX 62 76 {ECO:0000244|PDB:1U6G}.
HELIX 81 94 {ECO:0000244|PDB:1U6G}.
STRAND 98 100 {ECO:0000244|PDB:1U6G}.
HELIX 101 116 {ECO:0000244|PDB:1U6G}.
HELIX 127 142 {ECO:0000244|PDB:1U6G}.
HELIX 148 164 {ECO:0000244|PDB:1U6G}.
TURN 170 172 {ECO:0000244|PDB:1U6G}.
HELIX 173 180 {ECO:0000244|PDB:1U6G}.
HELIX 181 185 {ECO:0000244|PDB:1U6G}.
HELIX 189 202 {ECO:0000244|PDB:1U6G}.
TURN 203 205 {ECO:0000244|PDB:1U6G}.
HELIX 214 224 {ECO:0000244|PDB:1U6G}.
HELIX 234 244 {ECO:0000244|PDB:1U6G}.
HELIX 247 249 {ECO:0000244|PDB:1U6G}.
HELIX 256 264 {ECO:0000244|PDB:1U6G}.
TURN 269 271 {ECO:0000244|PDB:1U6G}.
HELIX 272 284 {ECO:0000244|PDB:1U6G}.
HELIX 291 301 {ECO:0000244|PDB:1U6G}.
HELIX 348 361 {ECO:0000244|PDB:1U6G}.
HELIX 368 372 {ECO:0000244|PDB:1U6G}.
TURN 373 375 {ECO:0000244|PDB:1U6G}.
HELIX 376 380 {ECO:0000244|PDB:1U6G}.
STRAND 386 388 {ECO:0000244|PDB:1U6G}.
HELIX 389 405 {ECO:0000244|PDB:1U6G}.
HELIX 424 431 {ECO:0000244|PDB:1U6G}.
HELIX 434 442 {ECO:0000244|PDB:1U6G}.
HELIX 448 464 {ECO:0000244|PDB:1U6G}.
TURN 466 469 {ECO:0000244|PDB:1U6G}.
HELIX 470 472 {ECO:0000244|PDB:1U6G}.
HELIX 473 483 {ECO:0000244|PDB:1U6G}.
STRAND 487 489 {ECO:0000244|PDB:1U6G}.
HELIX 491 506 {ECO:0000244|PDB:1U6G}.
HELIX 510 513 {ECO:0000244|PDB:1U6G}.
HELIX 514 517 {ECO:0000244|PDB:1U6G}.
TURN 518 520 {ECO:0000244|PDB:1U6G}.
HELIX 521 528 {ECO:0000244|PDB:1U6G}.
HELIX 533 550 {ECO:0000244|PDB:1U6G}.
STRAND 553 555 {ECO:0000244|PDB:1U6G}.
HELIX 562 576 {ECO:0000244|PDB:1U6G}.
STRAND 579 581 {ECO:0000244|PDB:1U6G}.
HELIX 583 599 {ECO:0000244|PDB:1U6G}.
HELIX 601 603 {ECO:0000244|PDB:1U6G}.
HELIX 607 618 {ECO:0000244|PDB:1U6G}.
STRAND 621 623 {ECO:0000244|PDB:1U6G}.
HELIX 624 635 {ECO:0000244|PDB:1U6G}.
HELIX 645 658 {ECO:0000244|PDB:1U6G}.
HELIX 664 680 {ECO:0000244|PDB:1U6G}.
HELIX 687 694 {ECO:0000244|PDB:1U6G}.
HELIX 698 700 {ECO:0000244|PDB:1U6G}.
HELIX 706 719 {ECO:0000244|PDB:1U6G}.
HELIX 724 729 {ECO:0000244|PDB:1U6G}.
TURN 730 734 {ECO:0000244|PDB:1U6G}.
HELIX 735 742 {ECO:0000244|PDB:1U6G}.
HELIX 749 763 {ECO:0000244|PDB:1U6G}.
HELIX 772 779 {ECO:0000244|PDB:1U6G}.
TURN 781 785 {ECO:0000244|PDB:1U6G}.
HELIX 793 809 {ECO:0000244|PDB:1U6G}.
HELIX 815 818 {ECO:0000244|PDB:1U6G}.
TURN 819 824 {ECO:0000244|PDB:1U6G}.
TURN 826 829 {ECO:0000244|PDB:1U6G}.
HELIX 832 848 {ECO:0000244|PDB:1U6G}.
HELIX 856 863 {ECO:0000244|PDB:1U6G}.
HELIX 864 866 {ECO:0000244|PDB:1U6G}.
HELIX 870 886 {ECO:0000244|PDB:1U6G}.
HELIX 888 900 {ECO:0000244|PDB:1U6G}.
HELIX 903 905 {ECO:0000244|PDB:1U6G}.
HELIX 906 918 {ECO:0000244|PDB:1U6G}.
TURN 923 925 {ECO:0000244|PDB:1U6G}.
HELIX 926 936 {ECO:0000244|PDB:1U6G}.
HELIX 947 960 {ECO:0000244|PDB:1U6G}.
HELIX 963 965 {ECO:0000244|PDB:1U6G}.
HELIX 967 970 {ECO:0000244|PDB:1U6G}.
TURN 971 973 {ECO:0000244|PDB:1U6G}.
STRAND 974 977 {ECO:0000244|PDB:1U6G}.
HELIX 979 988 {ECO:0000244|PDB:1U6G}.
HELIX 990 992 {ECO:0000244|PDB:1U6G}.
HELIX 1001 1007 {ECO:0000244|PDB:1U6G}.
TURN 1009 1014 {ECO:0000244|PDB:1U6G}.
STRAND 1015 1019 {ECO:0000244|PDB:1U6G}.
HELIX 1021 1036 {ECO:0000244|PDB:1U6G}.
HELIX 1038 1040 {ECO:0000244|PDB:1U6G}.
HELIX 1042 1044 {ECO:0000244|PDB:1U6G}.
HELIX 1045 1054 {ECO:0000244|PDB:1U6G}.
HELIX 1060 1062 {ECO:0000244|PDB:1U6G}.
STRAND 1063 1068 {ECO:0000244|PDB:1U6G}.
STRAND 1071 1076 {ECO:0000244|PDB:1U6G}.
HELIX 1079 1094 {ECO:0000244|PDB:1U6G}.
STRAND 1098 1100 {ECO:0000244|PDB:1U6G}.
HELIX 1102 1111 {ECO:0000244|PDB:1U6G}.
HELIX 1117 1132 {ECO:0000244|PDB:1U6G}.
HELIX 1136 1139 {ECO:0000244|PDB:1U6G}.
TURN 1140 1145 {ECO:0000244|PDB:1U6G}.
HELIX 1146 1154 {ECO:0000244|PDB:1U6G}.
HELIX 1163 1182 {ECO:0000244|PDB:1U6G}.
STRAND 1190 1194 {ECO:0000244|PDB:1U6G}.
HELIX 1200 1208 {ECO:0000244|PDB:1U6G}.
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


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