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Q6ZQ38 (CAND1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cullin-associated NEDD8-dissociated protein 1
Alternative name(s):
Cullin-associated and neddylation-dissociated protein 1
p120 CAND1
Gene names
Name:Cand1
Synonyms:D10Ertd516e, Kiaa0829
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1230 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

Subunit structure

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 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Predominantly cytoplasmic By similarity.

Sequence similarities

Belongs to the CAND family.

Contains 27 HEAT repeats.

Sequence caution

The sequence AAH57457.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB26438.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC98035.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 12301229Cullin-associated NEDD8-dissociated protein 1
PRO_0000089294

Regions

Repeat2 – 3938HEAT 1
Repeat44 – 8138HEAT 2
Repeat83 – 11937HEAT 3
Repeat131 – 16535HEAT 4
Repeat171 – 20838HEAT 5
Repeat210 – 24738HEAT 6
Repeat248 – 28235HEAT 7
Repeat289 – 36678HEAT 8
Repeat370 – 40738HEAT 9
Repeat424 – 46744HEAT 10
Repeat471 – 51040HEAT 11
Repeat515 – 55238HEAT 12
Repeat563 – 60240HEAT 13
Repeat606 – 64338HEAT 14
Repeat646 – 68338HEAT 15
Repeat688 – 72538HEAT 16
Repeat729 – 76840HEAT 17
Repeat770 – 80839HEAT 18
Repeat809 – 84537HEAT 19
Repeat852 – 88938HEAT 20
Repeat890 – 92738HEAT 21
Repeat928 – 96033HEAT 22
Repeat961 – 99838HEAT 23
Repeat1002 – 103938HEAT 24
Repeat1043 – 109755HEAT 25
Repeat1099 – 113335HEAT 26
Repeat1140 – 118950HEAT 27
Compositional bias314 – 34431Asp-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3351Phosphoserine By similarity
Modified residue9711N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6ZQ38 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: 20B6BFB4ED250825

FASTA1,230136,332
        10         20         30         40         50         60 
MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILRLLEDK 

        70         80         90        100        110        120 
NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE QLRDISSIGL KTVIGELPPA 

       130        140        150        160        170        180 
SSGSALAANV CKKITGRLTS AIAKQEDVSV QLEALDIMAD MLSRQGGLLV NFHPSILTCL 

       190        200        210        220        230        240 
LPQLTSPRLA VRKRTIIALG HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA 

       250        260        270        280        290        300 
ISRQAGHRIG EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI 

       310        320        330        340        350        360 
CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR RAAAKCLDAV 

       370        380        390        400        410        420 
VSTRHEMLPE FYKTVSPALI ARFKEREENV KADVFHAYLS LLKQTRPVQS WLCDPDAMEQ 

       430        440        450        460        470        480 
GDTPLTMLQS QVPNIVKALH KQMKEKSVKT RQCCFNMLTE LVNVLPGALT QHIPVLVPGI 

       490        500        510        520        530        540 
IFSLNDKSSS SNLKIDALSC LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL 

       550        560        570        580        590        600 
LVTQQLVKVI RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL 

       610        620        630        640        650        660 
GDNLGPDLSN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE GVPILASFLR 

       670        680        690        700        710        720 
KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL ISESDMHVSQ MAISFLTTLA 

       730        740        750        760        770        780 
KVYPSSLSKI SGSILNELIG LVRSPLLQGG ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT 

       790        800        810        820        830        840 
GPVYSQSTAL THKQSYYSIA KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL 

       850        860        870        880        890        900 
SLGEVGHHID LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT 

       910        920        930        940        950        960 
SQPKRQYLLL HSLKEIISSA SVAGLKPYVE NIWALLLKHC ECAEEGTRNV VAECLGKLTL 

       970        980        990       1000       1010       1020 
IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI DPLLKNCIGD FLKTLEDPDL 

      1030       1040       1050       1060       1070       1080 
NVRRVALVTF NSAAHNKPSL IRDLLDSVLP HLYNETKVRK ELIREVEMGP FKHTVDDGLD 

      1090       1100       1110       1120       1130       1140 
IRKAAFECMY TLLDSCLDRL DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ 

      1150       1160       1170       1180       1190       1200 
RLDRLVEPLR ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS 

      1210       1220       1230 
QISSNPELAA IFESIQKDSS STNLESMDTS 

« Hide

References

[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryonic tail.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 342-1230.
Strain: FVB/N.
Tissue: Kidney.
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1007-1230.
Strain: C57BL/6J.
Tissue: Tongue.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK129225 mRNA. Translation: BAC98035.1. Different initiation.
BC057457 mRNA. Translation: AAH57457.1. Different initiation.
AK009683 mRNA. Translation: BAB26438.1. Different initiation.
RefSeqNP_082270.1. NM_027994.1.
UniGeneMm.203965.

3D structure databases

ProteinModelPortalQ6ZQ38.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215017. 2 interactions.
IntActQ6ZQ38. 5 interactions.
MINTMINT-1862433.

PTM databases

PhosphoSiteQ6ZQ38.

Proteomic databases

PaxDbQ6ZQ38.
PRIDEQ6ZQ38.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020315; ENSMUSP00000020315; ENSMUSG00000020114.
GeneID71902.
KEGGmmu:71902.
UCSCuc007hec.2. mouse.

Organism-specific databases

CTD55832.
MGIMGI:1261820. Cand1.
RougeSearch...

Phylogenomic databases

eggNOGNOG278162.
GeneTreeENSGT00390000017740.
HOGENOMHOG000264713.
HOVERGENHBG053467.
InParanoidQ6ZQ38.
KOK17263.
OMAAIACMGQ.
OrthoDBEOG77HDCZ.
PhylomeDBQ6ZQ38.
TreeFamTF300355.

Gene expression databases

ArrayExpressQ6ZQ38.
BgeeQ6ZQ38.
CleanExMM_CAND1.
GenevestigatorQ6ZQ38.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013932. TATA-bd_TIP120.
[Graphical view]
PfamPF08623. TIP120. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

NextBio334892.
PROQ6ZQ38.
SOURCESearch...

Entry information

Entry nameCAND1_MOUSE
AccessionPrimary (citable) accession number: Q6ZQ38
Secondary accession number(s): Q6PFR0, Q9CV45
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot