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DCN1-like protein 1 (DCUN1 domain-containing protein 1) (Defective in cullin neddylation protein 1-like protein 1) (Testis-specific protein 3)

 DCNL1_MOUSE             Reviewed;         259 AA.
Q9QZ73; Q3TMX2; Q8CDZ7;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-JUN-2018, entry version 132.
RecName: Full=DCN1-like protein 1;
AltName: Full=DCUN1 domain-containing protein 1;
AltName: Full=Defective in cullin neddylation protein 1-like protein 1;
AltName: Full=Testis-specific protein 3;
Name=Dcun1d1; Synonyms=Dcun1l1, Rp42, Tes3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=10831844; DOI=10.1016/S0378-1119(00)00158-X;
Pourcel C., Jaubert J., Hadchouel M., Wu X., Schweizer J.;
"A new family of genes and pseudogenes potentially expressing testis-
specific and brain-specific leucine-zipper proteins in man and
mouse.";
Gene 249:105-113(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Telencephalon;
PubMed=10777668; DOI=10.1006/geno.2000.6126;
Mas C., Bourgeois F., Bulfone A., Levacher B., Mugnier C.,
Simonneau M.;
"Cloning and expression analysis of a novel gene, RP42, mapping to an
autism susceptibility locus on 6q16.";
Genomics 65:70-74(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Colon, Head, and Stomach;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary tumor;
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).
[5]
DEVELOPMENTAL STAGE, AND FUNCTION.
PubMed=20563250; DOI=10.1593/neo.10202;
Broderick S.R., Golas B.J., Pham D., Towe C.W., Talbot S.G.,
Kaufman A., Bains S., Huryn L.A., Yonekawa Y., Carlson D.,
Hambardzumyan D., Ramanathan Y., Singh B.;
"SCCRO promotes glioma formation and malignant progression in mice.";
Neoplasia 12:476-484(2010).
-!- FUNCTION: Part of an E3 ubiquitin ligase complex for neddylation.
Promotes neddylation of cullin components of E3 cullin-RING
ubiquitin ligase complexes. Acts by binding to cullin-RBX1
complexes in the cytoplasm and promoting their nuclear
translocation, enhancing recruitment of E2-NEDD8 (UBE2M-NEDD8)
thioester to the complex, and optimizing the orientation of
proteins in the complex to allow efficient transfer of NEDD8 from
the E2 to the cullin substrates. Involved in the release of
inhibitory effets of CAND1 on cullin-RING ligase E3 complex
assembly and activity (By similarity). Acts also as an oncogene
facilitating malignant transformation and carcinogenic in vivo
(PubMed:20563250). {ECO:0000250|UniProtKB:Q96GG9,
ECO:0000269|PubMed:20563250}.
-!- SUBUNIT: Part of an E3 complex for neddylation composed of
cullins, RBX1, UBE2M and CAND1. Interacts (via the C-terminus 50
AA) with CUL1, CUL2, CUL3, CUL4 and CUL5. Binds neddylated CUL1.
Interacts (via the C-terminus 50 AA) directly with RBX1. Interacts
(via DCUN1 domain) with UBE2M (acetylated at N-terminal
methionine). Interacts preferentially with UBE2M-NEDD8 thioester
(via N-terminus 1-26 AA) than with free UBE2M. UBE2M N-terminal
acetylation increases the affinity of this interaction by about 2
orders of magnitude. Interacts with CAND1 when in complex with
CUL1-RBX1. {ECO:0000250|UniProtKB:Q96GG9}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96GG9}.
-!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in
brain, heart, liver, skeletal muscle and kidney. In brain,
preferentially expressed in the telencephalon ventricular and
subventricular zones, albeit at low levels. In adult testis,
expressed in cells above seminiferous tubules, but only weakly in
spermatogonia. {ECO:0000269|PubMed:10777668,
ECO:0000269|PubMed:10831844}.
-!- DEVELOPMENTAL STAGE: Expressed in the developing forebrain,
midbrain and hindbrain at early stages of neuronal development.
{ECO:0000269|PubMed:20563250}.
-!- DOMAIN: The DCUN1 domain, also known as PONY domain mediates its
interaction with N-terminally acetylated UBE2M.
{ECO:0000250|UniProtKB:Q96GG9}.
-!- SEQUENCE CAUTION:
Sequence=BAC26390.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF198092; AAF04863.1; -; mRNA.
EMBL; AK008657; BAB25813.1; -; mRNA.
EMBL; AK029314; BAC26390.1; ALT_INIT; mRNA.
EMBL; AK155081; BAE33033.1; -; mRNA.
EMBL; AK165651; BAE38318.1; -; mRNA.
EMBL; BC020161; AAH20161.1; -; mRNA.
EMBL; BC031666; AAH31666.1; -; mRNA.
EMBL; BC037431; AAH37431.1; -; mRNA.
CCDS; CCDS57207.1; -.
RefSeq; NP_001192290.1; NM_001205361.1.
UniGene; Mm.374810; -.
UniGene; Mm.379305; -.
UniGene; Mm.441473; -.
UniGene; Mm.445013; -.
UniGene; Mm.474495; -.
ProteinModelPortal; Q9QZ73; -.
SMR; Q9QZ73; -.
STRING; 10090.ENSMUSP00000103817; -.
iPTMnet; Q9QZ73; -.
PhosphoSitePlus; Q9QZ73; -.
EPD; Q9QZ73; -.
MaxQB; Q9QZ73; -.
PaxDb; Q9QZ73; -.
PRIDE; Q9QZ73; -.
DNASU; 114893; -.
Ensembl; ENSMUST00000108182; ENSMUSP00000103817; ENSMUSG00000027708.
GeneID; 114893; -.
KEGG; mmu:114893; -.
UCSC; uc008oyw.2; mouse.
CTD; 54165; -.
MGI; MGI:2150386; Dcun1d1.
eggNOG; KOG3077; Eukaryota.
eggNOG; ENOG410XTIJ; LUCA.
GeneTree; ENSGT00550000074529; -.
HOGENOM; HOG000241761; -.
HOVERGEN; HBG055256; -.
InParanoid; Q9QZ73; -.
KO; K17822; -.
OMA; MITDDMS; -.
OrthoDB; EOG091G0HHH; -.
PhylomeDB; Q9QZ73; -.
PRO; PR:Q9QZ73; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027708; -.
ExpressionAtlas; Q9QZ73; baseline and differential.
Genevisible; Q9QZ73; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
GO; GO:0032182; F:ubiquitin-like protein binding; IBA:GO_Central.
GO; GO:2000436; P:positive regulation of protein neddylation; ISS:UniProtKB.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IBA:GO_Central.
GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
InterPro; IPR014764; DCN-prot.
InterPro; IPR005176; PONY_dom.
InterPro; IPR009060; UBA-like_sf.
PANTHER; PTHR12281; PTHR12281; 1.
Pfam; PF03556; Cullin_binding; 1.
SUPFAM; SSF46934; SSF46934; 1.
PROSITE; PS51229; DCUN1; 1.
2: Evidence at transcript level;
Acetylation; Complete proteome; Nucleus; Proto-oncogene;
Reference proteome; Ubl conjugation pathway.
CHAIN 1 259 DCN1-like protein 1.
/FTId=PRO_0000129499.
DOMAIN 8 45 UBA-like.
DOMAIN 60 248 DCUN1. {ECO:0000255|PROSITE-
ProRule:PRU00574}.
SITE 115 115 Essential for interaction with UBE2M.
{ECO:0000250|UniProtKB:Q96GG9}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q96GG9}.
CONFLICT 13 13 R -> S (in Ref. 3; BAC26390).
{ECO:0000305}.
CONFLICT 115 115 C -> F (in Ref. 3; BAC26390).
{ECO:0000305}.
CONFLICT 259 259 V -> L (in Ref. 3; BAC26390).
{ECO:0000305}.
SEQUENCE 259 AA; 30097 MW; 06E095D5F58EF20A CRC64;
MNKLKSSQKD KVRQFMIFTQ SSEKTAVSCL SQNDWKLDVA TDNFFQNPEL YIRESVKGSL
DRKKLEQLYT RYKDPQDENK IGIDGIQQFC DDLALDPASI SVLIIAWKFR AATQCEFSKQ
EFMDGMTELG CDSIEKLKAQ IPKMEQELKE PGRFKDFYQF TFNFAKNPGQ KGLDLEMAIA
YWNLVLNGRF KFLDLWNKFL LEHHKRSIPK DTWNLLLDFS SMIADDMSNY DEEGAWPVLI
DDFVEFARPQ IAGTKSTTV


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