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Q86VP6 (CAND1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
TBP-interacting protein of 120 kDa A
Short name=TBP-interacting protein 120A
p120 CAND1
Gene names
Name:CAND1
Synonyms:KIAA0829, TIP120, TIP120A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1230 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.21 Ref.24

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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.20 Ref.21

Subcellular location

Cytoplasm. Nucleus. Note: Predominantly cytoplasmic. Ref.21

Induction

Repressed by miR-148a. Ref.18

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 (Ref.24).

Sequence similarities

Belongs to the CAND family.

Contains 27 HEAT repeats.

Sequence caution

The sequence BAA74852.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB55090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86VP6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q86VP6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     458-625: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q86VP6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.
     549-560: VIRPLDQPSSFD → AHHMPEAQWLRL
     561-1230: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9
Chain2 – 12301229Cullin-associated NEDD8-dissociated protein 1
PRO_0000089293

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 Ref.8 Ref.9 Ref.16 Ref.22
Modified residue551N6-acetyllysine Ref.17
Modified residue3351Phosphoserine Ref.14
Modified residue9711N6-acetyllysine Ref.17

Natural variations

Alternative sequence1 – 157157Missing in isoform 3.
VSP_013947
Alternative sequence458 – 625168Missing in isoform 2.
VSP_013948
Alternative sequence549 – 56012VIRPL…PSSFD → AHHMPEAQWLRL in isoform 3.
VSP_013949
Alternative sequence561 – 1230670Missing in isoform 3.
VSP_013950
Natural variant8031V → A.
Corresponds to variant rs12580996 [ dbSNP | Ensembl ].
VAR_054041
Natural variant9521A → V. Ref.6
Corresponds to variant rs17854618 [ dbSNP | Ensembl ].
VAR_025327

Experimental info

Sequence conflict2721R → K in BAB55365. Ref.7
Sequence conflict4571M → I in BAB55090. Ref.7
Sequence conflict6061S → P in AAF67492. Ref.3
Sequence conflict6091P → S in AAF67492. Ref.3
Sequence conflict10471T → S in AAF67492. Ref.3
Sequence conflict11771M → T in BAB55090. Ref.7

Secondary structure

.............................................................................................................................................................................. 1230
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: FE344558F72D79D8

FASTA1,230136,376
        10         20         30         40         50         60 
MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILKLLEDK 

        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 SRFKEREENV KADVFHAYLS LLKQTRPVQS WLCDPDAMEQ 

       430        440        450        460        470        480 
GETPLTMLQS 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 
GDNLGSDLPN 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 SVVGLKPYVE NIWALLLKHC ECAEEGTRNV VAECLGKLTL 

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

      1030       1040       1050       1060       1070       1080 
NVRRVALVTF NSAAHNKPSL IRDLLDTVLP 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

Isoform 2 [UniParc].

Checksum: 2045EBFCEE84468B
Show »

FASTA1,062117,889
Isoform 3 [UniParc].

Checksum: 4EC2B75A93D82663
Show »

FASTA40345,539

References

« Hide 'large scale' references
[1]"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."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
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. expand/collapse author list , 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.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adrenal gland.
[4]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Testis.
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1), VARIANT VAL-952.
Tissue: Cervix, Testis and Uterus.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Placenta.
[8]Bienvenut W.V., Ramsay A., Leung H.Y.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14 AND 374-382, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[9]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[10]"CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex."
Zheng J., Yang X., Harrell J.M., Ryzhikov S., Shim E.-H., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H.
Mol. Cell 10:1519-1526(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1 AND RBX1.
[11]"NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases."
Liu J., Furukawa M., Matsumoto T., Xiong Y.
Mol. Cell 10:1511-1518(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1 AND RBX1, INTERACTION WITH UNNEDDYLATED CUL1; CUL4A AND CUL5.
[12]"TIP120A associates with cullins and modulates ubiquitin ligase activity."
Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.
J. Biol. Chem. 278:15905-15910(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B AND RBX1, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"CAND1-mediated substrate adaptor recycling is required for efficient repression of Nrf2 by Keap1."
Lo S.C., Hannink M.
Mol. Cell. Biol. 26:1235-1244(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CUL3.
[14]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-971, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"miR-148a is an androgen-responsive microRNA that promotes LNCaP prostate cell growth by repressing its target CAND1 expression."
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.
Prostate Cancer Prostatic Dis. 13:356-361(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding."
Mao X., Gluck N., Chen B., Starokadomskyy P., Li H., Maine G.N., Burstein E.
J. Biol. Chem. 286:32355-32365(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CUL2.
[21]"Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo."
Chua Y.S., Boh B.K., Ponyeam W., Hagen T.
PLoS ONE 6:E16071-E16071(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CUL2; CUL3; CUL4A AND CUL5, SUBCELLULAR LOCATION.
[22]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins."
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.
Cell 153:206-215(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, REACTION MECHANISM.
[25]"Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases."
Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J., Xiong Y., Zheng N.
Cell 119:517-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CUL1 AND RBX1.
[26]"The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation."
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.
Cell 147:1024-1039(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEX WITH CUL4B AND RBX1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB020636 mRNA. Translation: BAA74852.2. Different initiation.
AF157326 mRNA. Translation: AAF67492.1.
AL133560 mRNA. Translation: CAB63714.1.
AL136810 mRNA. Translation: CAB66744.1.
AL833880 mRNA. Translation: CAD38737.1.
CH471054 Genomic DNA. Translation: EAW97172.1.
BC004232 mRNA. Translation: AAH04232.1.
BC026220 mRNA. Translation: AAH26220.1.
BC050341 mRNA. Translation: AAH50341.1.
AK027404 mRNA. Translation: BAB55090.1. Different initiation.
AK027783 mRNA. Translation: BAB55365.1.
AK314358 mRNA. Translation: BAG36990.1.
PIRT43441.
RefSeqNP_060918.2. NM_018448.3.
UniGeneHs.546407.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U6GX-ray3.10C1-1230[»]
4A0CX-ray3.80A/B1-1230[»]
ProteinModelPortalQ86VP6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120937. 673 interactions.
DIPDIP-31608N.
IntActQ86VP6. 15 interactions.
MINTMINT-4999459.

PTM databases

PhosphoSiteQ86VP6.

Polymorphism databases

DMDM67460541.

Proteomic databases

PaxDbQ86VP6.
PRIDEQ86VP6.

Protocols and materials databases

DNASU55832.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000544619; ENSP00000444089; ENSG00000111530.
ENST00000545606; ENSP00000442318; ENSG00000111530. [Q86VP6-1]
GeneID55832.
KEGGhsa:55832.
UCSCuc001stn.2. human. [Q86VP6-1]
uc001sto.2. human. [Q86VP6-2]

Organism-specific databases

CTD55832.
GeneCardsGC12P067663.
HGNCHGNC:30688. CAND1.
HPAHPA055748.
MIM607727. gene.
neXtProtNX_Q86VP6.
PharmGKBPA142672207.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278162.
HOVERGENHBG053467.
InParanoidQ86VP6.
KOK17263.
OMAAIACMGQ.
OrthoDBEOG77HDCZ.
PhylomeDBQ86VP6.
TreeFamTF300355.

Gene expression databases

ArrayExpressQ86VP6.
BgeeQ86VP6.
GenevestigatorQ86VP6.

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

ChiTaRSCAND1. human.
EvolutionaryTraceQ86VP6.
GeneWikiCAND1.
GenomeRNAi55832.
NextBio61049.
PROQ86VP6.
SOURCESearch...

Entry information

Entry nameCAND1_HUMAN
AccessionPrimary (citable) accession number: Q86VP6
Secondary accession number(s): B2RAU3 expand/collapse secondary AC list , O94918, Q6PIY4, Q8NDJ4, Q96JZ9, Q96T19, Q9BTC4, Q9H0G2, Q9P0H7, Q9UF85
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM