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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_RAT               Reviewed;        1230 AA.
P97536;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
07-NOV-2018, entry version 123.
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=Tip120, Tip120a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH
TBP, AND SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=8954946; DOI=10.1006/bbrc.1996.1852;
Yogosawa S., Makino Y., Yoshida T., Kishimoto T., Muramatsu M.,
Tamura T.-A.;
"Molecular cloning of a novel 120-kDa TBP-interacting protein.";
Biochem. Biophys. Res. Commun. 229:612-617(1996).
[2]
TISSUE SPECIFICITY.
PubMed=10441524; DOI=10.1006/bbrc.1999.1147;
Aoki T., Okada N., Ishida M., Yogosawa S., Makino Y., Tamura T.-A.;
"TIP120B: a novel TIP120-family protein that is expressed specifically
in muscle tissues.";
Biochem. Biophys. Res. Commun. 261:911-916(1999).
[3]
FUNCTION.
PubMed=10567521; DOI=10.1128/MCB.19.12.7951;
Makino Y., Yogosawa S., Kayukawa K., Coin F., Egly J.-M., Wang Z.-X.,
Roeder R.G., Yamamoto K., Muramatsu M., Tamura T.-A.;
"TATA-Binding protein-interacting protein 120, TIP120, stimulates
three classes of eukaryotic transcription via a unique mechanism.";
Mol. Cell. Biol. 19:7951-7960(1999).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-558, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 (By similarity). May
indirectly enhance transcription from various types of promoters.
{ECO:0000250, ECO:0000269|PubMed:10567521}.
-!- SUBUNIT: 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 (By similarity). Interacts with
TBP. Interacts with DCUN1D3 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q86VP6, ECO:0000269|PubMed:8954946}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:8954946}. Note=Predominantly cytoplasmic.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in heart, brain, spleen, liver,
skeletal muscle, kidney and testis. {ECO:0000269|PubMed:10441524}.
-!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D87671; BAA13432.1; -; mRNA.
PIR; T42735; T42735.
RefSeq; NP_446456.1; NM_054004.2.
UniGene; Rn.32934; -.
ProteinModelPortal; P97536; -.
SMR; P97536; -.
BioGrid; 250683; 4.
IntAct; P97536; 1.
STRING; 10116.ENSRNOP00000010720; -.
iPTMnet; P97536; -.
PhosphoSitePlus; P97536; -.
PaxDb; P97536; -.
PRIDE; P97536; -.
Ensembl; ENSRNOT00000010720; ENSRNOP00000010720; ENSRNOG00000007834.
GeneID; 117152; -.
KEGG; rno:117152; -.
UCSC; RGD:620479; rat.
CTD; 55832; -.
RGD; 620479; Cand1.
eggNOG; KOG1824; Eukaryota.
eggNOG; ENOG410XPK4; LUCA.
GeneTree; ENSGT00390000017740; -.
HOGENOM; HOG000264713; -.
HOVERGEN; HBG053467; -.
InParanoid; P97536; -.
KO; K17263; -.
OMA; MASHQYH; -.
OrthoDB; EOG091G017Q; -.
PhylomeDB; P97536; -.
Reactome; R-RNO-6798695; Neutrophil degranulation.
Reactome; R-RNO-8951664; Neddylation.
Reactome; R-RNO-917937; Iron uptake and transport.
PRO; PR:P97536; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000007834; Expressed in 10 organ(s), highest expression level in testis.
Genevisible; P97536; RN.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0017025; F:TBP-class protein binding; IDA:RGD.
GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:0010265; P:SCF complex assembly; ISS:UniProtKB.
Gene3D; 1.25.10.10; -; 2.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR039852; CAND1/CAND2.
InterPro; IPR013932; TATA-bd_TIP120.
PANTHER; PTHR12696; PTHR12696; 1.
Pfam; PF08623; TIP120; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q86VP6}.
CHAIN 2 1230 Cullin-associated NEDD8-dissociated
protein 1.
/FTId=PRO_0000089296.
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:0000250|UniProtKB:Q86VP6}.
MOD_RES 55 55 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q86VP6}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 971 971 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q86VP6}.
SEQUENCE 1230 AA; 136362 MW; A3ACF0E99B99A1D7 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
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 SVVGLKPYVE 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


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