ID   CAND1_MOUSE             Reviewed;        1230 AA.
AC   Q6ZQ38; Q6PFR0; Q9CV45;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Cullin-associated NEDD8-dissociated protein 1;
DE   AltName: Full=Cullin-associated and neddylation-dissociated protein 1;
DE   AltName: Full=p120 CAND1;
GN   Name=Cand1; Synonyms=D10Ertd516e, Kiaa0829;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 342-1230.
RC   STRAIN=FVB/N; TISSUE=Kidney;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1007-1230.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3
CC       ubiquitin ligase complexes that promotes the exchange of the substrate-
CC       recognition F-box subunit in SCF complexes, thereby playing a key role
CC       in the cellular repertoire of SCF complexes. Acts as a F-box protein
CC       exchange factor. The exchange activity of CAND1 is coupled with cycles
CC       of neddylation conjugation: in the deneddylated state, cullin-binding
CC       CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and
CC       promoting exchange of the F-box protein. Probably plays a similar role
CC       in other cullin-RING E3 ubiquitin ligase complexes (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TBP (By similarity). Part of a complex that
CC       contains CUL1 and RBX1. Interacts with unneddylated cullins: interacts
CC       with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5. Does not bind neddylated
CC       CUL1. Interaction with cullins is abolished in presence of COMMD1,
CC       which antagonizes with CAND1 for interacting with cullins. Interacts
CC       with ERCC6 (By similarity). Interacts with DCUN1D1, DCUN1D2, DCUN1D3,
CC       DCUN1D4 and DCUN1D5; these interactions are bridged by cullins and
CC       strongly inhibits the neddylation of cullins (By similarity).
CC       {ECO:0000250|UniProtKB:P97536, ECO:0000250|UniProtKB:Q86VP6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86VP6}. Nucleus
CC       {ECO:0000250|UniProtKB:Q86VP6}. Note=Predominantly cytoplasmic.
CC       {ECO:0000250|UniProtKB:Q86VP6}.
CC   -!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH57457.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB26438.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC98035.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK129225; BAC98035.1; ALT_INIT; mRNA.
DR   EMBL; BC057457; AAH57457.1; ALT_INIT; mRNA.
DR   EMBL; AK009683; BAB26438.1; ALT_INIT; mRNA.
DR   CCDS; CCDS48701.1; -.
DR   RefSeq; NP_082270.1; NM_027994.1.
DR   AlphaFoldDB; Q6ZQ38; -.
DR   SMR; Q6ZQ38; -.
DR   BioGRID; 215017; 40.
DR   IntAct; Q6ZQ38; 12.
DR   MINT; Q6ZQ38; -.
DR   STRING; 10090.ENSMUSP00000020315; -.
DR   GlyGen; Q6ZQ38; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6ZQ38; -.
DR   MetOSite; Q6ZQ38; -.
DR   PhosphoSitePlus; Q6ZQ38; -.
DR   SwissPalm; Q6ZQ38; -.
DR   EPD; Q6ZQ38; -.
DR   jPOST; Q6ZQ38; -.
DR   MaxQB; Q6ZQ38; -.
DR   PaxDb; 10090-ENSMUSP00000020315; -.
DR   PeptideAtlas; Q6ZQ38; -.
DR   ProteomicsDB; 265526; -.
DR   Pumba; Q6ZQ38; -.
DR   Antibodypedia; 16667; 242 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000020315.13; ENSMUSP00000020315.7; ENSMUSG00000020114.13.
DR   GeneID; 71902; -.
DR   KEGG; mmu:71902; -.
DR   UCSC; uc007hec.2; mouse.
DR   AGR; MGI:1261820; -.
DR   CTD; 55832; -.
DR   MGI; MGI:1261820; Cand1.
DR   VEuPathDB; HostDB:ENSMUSG00000020114; -.
DR   eggNOG; KOG1824; Eukaryota.
DR   GeneTree; ENSGT00390000017740; -.
DR   HOGENOM; CLU_007157_0_0_1; -.
DR   InParanoid; Q6ZQ38; -.
DR   OMA; AYIPHFQ; -.
DR   OrthoDB; 68829at2759; -.
DR   PhylomeDB; Q6ZQ38; -.
DR   TreeFam; TF300355; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   Reactome; R-MMU-917937; Iron uptake and transport.
DR   BioGRID-ORCS; 71902; 24 hits in 81 CRISPR screens.
DR   ChiTaRS; Cand1; mouse.
DR   PRO; PR:Q6ZQ38; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q6ZQ38; Protein.
DR   Bgee; ENSMUSG00000020114; Expressed in spermatocyte and 267 other cell types or tissues.
DR   ExpressionAtlas; Q6ZQ38; baseline and differential.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; ISO:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0010265; P:SCF complex assembly; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039852; CAND1/CAND2.
DR   InterPro; IPR013932; TATA-bd_TIP120.
DR   PANTHER; PTHR12696:SF1; CULLIN-ASSOCIATED NEDD8-DISSOCIATED PROTEIN 1; 1.
DR   PANTHER; PTHR12696; TIP120; 1.
DR   Pfam; PF13513; HEAT_EZ; 1.
DR   Pfam; PF08623; TIP120; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   Genevisible; Q6ZQ38; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q86VP6"
FT   CHAIN           2..1230
FT                   /note="Cullin-associated NEDD8-dissociated protein 1"
FT                   /id="PRO_0000089294"
FT   REPEAT          2..39
FT                   /note="HEAT 1"
FT   REPEAT          44..81
FT                   /note="HEAT 2"
FT   REPEAT          83..119
FT                   /note="HEAT 3"
FT   REPEAT          131..165
FT                   /note="HEAT 4"
FT   REPEAT          171..208
FT                   /note="HEAT 5"
FT   REPEAT          210..247
FT                   /note="HEAT 6"
FT   REPEAT          248..282
FT                   /note="HEAT 7"
FT   REPEAT          289..366
FT                   /note="HEAT 8"
FT   REPEAT          370..407
FT                   /note="HEAT 9"
FT   REPEAT          424..467
FT                   /note="HEAT 10"
FT   REPEAT          471..510
FT                   /note="HEAT 11"
FT   REPEAT          515..552
FT                   /note="HEAT 12"
FT   REPEAT          563..602
FT                   /note="HEAT 13"
FT   REPEAT          606..643
FT                   /note="HEAT 14"
FT   REPEAT          646..683
FT                   /note="HEAT 15"
FT   REPEAT          688..725
FT                   /note="HEAT 16"
FT   REPEAT          729..768
FT                   /note="HEAT 17"
FT   REPEAT          770..808
FT                   /note="HEAT 18"
FT   REPEAT          809..845
FT                   /note="HEAT 19"
FT   REPEAT          852..889
FT                   /note="HEAT 20"
FT   REPEAT          890..927
FT                   /note="HEAT 21"
FT   REPEAT          928..960
FT                   /note="HEAT 22"
FT   REPEAT          961..998
FT                   /note="HEAT 23"
FT   REPEAT          1002..1039
FT                   /note="HEAT 24"
FT   REPEAT          1043..1097
FT                   /note="HEAT 25"
FT   REPEAT          1099..1133
FT                   /note="HEAT 26"
FT   REPEAT          1140..1189
FT                   /note="HEAT 27"
FT   REGION          315..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..342
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86VP6"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86VP6"
FT   MOD_RES         558
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         971
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86VP6"
SQ   SEQUENCE   1230 AA;  136332 MW;  20B6BFB4ED250825 CRC64;
     MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILRLLEDK
     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 ARFKEREENV KADVFHAYLS LLKQTRPVQS WLCDPDAMEQ
     GDTPLTMLQS QVPNIVKALH KQMKEKSVKT RQCCFNMLTE LVNVLPGALT QHIPVLVPGI
     IFSLNDKSSS SNLKIDALSC LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL
     LVTQQLVKVI RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL
     GDNLGPDLSN 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 SVAGLKPYVE NIWALLLKHC ECAEEGTRNV VAECLGKLTL
     IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI DPLLKNCIGD FLKTLEDPDL
     NVRRVALVTF NSAAHNKPSL IRDLLDSVLP HLYNETKVRK ELIREVEMGP FKHTVDDGLD
     IRKAAFECMY TLLDSCLDRL DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ
     RLDRLVEPLR ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS
     QISSNPELAA IFESIQKDSS STNLESMDTS
//