Q86VP6 (CAND1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1230 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.20 Ref.21
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.18 Ref.20
Subcellular location	Cytoplasm. Nucleus. Note: Predominantly cytoplasmic. Ref.20
Induction	Repressed by miR-148a. Ref.17
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.21).
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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SCF complex assembly Inferred from direct assay Ref.22Ref.20. Source: UniProtKB cell differentiation Inferred from direct assay PubMed 10581176. Source: UniProtKB negative regulation of catalytic activity Inferred from direct assay Ref.12. Source: UniProtKB positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Inferred from electronic annotation. Source: Compara protein ubiquitination Inferred from direct assay Ref.12Ref.22Ref.20. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cullin-RING ubiquitin ligase complex Inferred from direct assay Ref.22Ref.20. Source: UniProtKB cytoplasm Inferred from direct assay Ref.20. Source: UniProtKB nucleus Inferred from direct assay PubMed 10581176Ref.20. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CUL1	Q13616	18	EBI-456077,EBI-359390
CUL2	Q13617	3	EBI-456077,EBI-456179
CUL3	Q13618	2	EBI-456077,EBI-456129
CUL4A	Q13619	3	EBI-456077,EBI-456106
CUL4B	Q13620	3	EBI-456077,EBI-456067

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8 Ref.9

Chain

2 – 1230

1229

Cullin-associated NEDD8-dissociated protein 1

PRO_0000089293

Regions

Repeat

2 – 39

38

HEAT 1

Repeat

44 – 81

38

HEAT 2

Repeat

83 – 119

37

HEAT 3

Repeat

131 – 165

35

HEAT 4

Repeat

171 – 208

38

HEAT 5

Repeat

210 – 247

38

HEAT 6

Repeat

248 – 282

35

HEAT 7

Repeat

289 – 366

78

HEAT 8

Repeat

370 – 407

38

HEAT 9

Repeat

424 – 467

44

HEAT 10

Repeat

471 – 510

40

HEAT 11

Repeat

515 – 552

38

HEAT 12

Repeat

563 – 602

40

HEAT 13

Repeat

606 – 643

38

HEAT 14

Repeat

646 – 683

38

HEAT 15

Repeat

688 – 725

38

HEAT 16

Repeat

729 – 768

40

HEAT 17

Repeat

770 – 808

39

HEAT 18

Repeat

809 – 845

37

HEAT 19

Repeat

852 – 889

38

HEAT 20

Repeat

890 – 927

38

HEAT 21

Repeat

928 – 960

33

HEAT 22

Repeat

961 – 998

38

HEAT 23

Repeat

1002 – 1039

38

HEAT 24

Repeat

1043 – 1097

55

HEAT 25

Repeat

1099 – 1133

35

HEAT 26

Repeat

1140 – 1189

50

HEAT 27

Compositional bias

314 – 344

31

Asp-rich

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8 Ref.9

Modified residue

55

1

N6-acetyllysine Ref.16

Modified residue

335

1

Phosphoserine Ref.14

Modified residue

971

1

N6-acetyllysine Ref.16

Natural variations

Alternative sequence

1 – 157

157

Missing in isoform 3.

VSP_013947

Alternative sequence

458 – 625

168

Missing in isoform 2.

VSP_013948

Alternative sequence

549 – 560

12

VIRPL…PSSFD → AHHMPEAQWLRL in isoform 3.

VSP_013949

Alternative sequence

561 – 1230

670

Missing in isoform 3.

VSP_013950

Natural variant

803

1

V → A.
Corresponds to variant rs12580996 [ dbSNP | Ensembl ].

VAR_054041

Natural variant

952

1

A → V. Ref.6
Corresponds to variant rs17854618 [ dbSNP | Ensembl ].

VAR_025327

Experimental info

Sequence conflict

272

1

R → K in BAB55365. Ref.7

Sequence conflict

457

1

M → I in BAB55090. Ref.7

Sequence conflict

606

1

S → P in AAF67492. Ref.3

Sequence conflict

609

1

P → S in AAF67492. Ref.3

Sequence conflict

1047

1

T → S in AAF67492. Ref.3

Sequence conflict

1177

1

M → T in BAB55090. Ref.7

Secondary structure

1

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1230

Helix Strand Turn

Details...

Helix

6 – 14

9

Helix

20 – 33

14

Beta strand

35 – 37

3

Helix

45 – 56

12

Helix

62 – 76

15

Helix

81 – 94

14

Beta strand

98 – 100

3

Helix

101 – 116

16

Helix

127 – 142

16

Helix

148 – 164

17

Turn

170 – 172

3

Helix

173 – 180

8

Helix

181 – 185

5

Helix

189 – 202

14

Turn

203 – 205

3

Helix

214 – 224

11

Helix

234 – 244

11

Helix

247 – 249

3

Helix

256 – 264

9

Turn

269 – 271

3

Helix

272 – 284

13

Helix

291 – 301

11

Helix

348 – 361

14

Helix

368 – 372

5

Turn

373 – 375

3

Helix

376 – 380

5

Beta strand

386 – 388

3

Helix

389 – 405

17

Helix

424 – 431

8

Helix

434 – 442

9

Helix

448 – 464

17

Turn

466 – 469

4

Helix

470 – 472

3

Helix

473 – 483

11

Beta strand

487 – 489

3

Helix

491 – 506

16

Helix

510 – 513

4

Helix

514 – 517

4

Turn

518 – 520

3

Helix

521 – 528

8

Helix

533 – 550

18

Beta strand

553 – 555

3

Helix

562 – 576

15

Beta strand

579 – 581

3

Helix

583 – 599

17

Helix

601 – 603

3

Helix

607 – 618

12

Beta strand

621 – 623

3

Helix

624 – 635

12

Helix

645 – 658

14

Helix

664 – 680

17

Helix

687 – 694

8

Helix

698 – 700

3

Helix

706 – 719

14

Helix

724 – 729

6

Turn

730 – 734

5

Helix

735 – 742

8

Helix

749 – 763

15

Helix

772 – 779

8

Turn

781 – 785

5

Helix

793 – 809

17

Helix

815 – 818

4

Turn

819 – 824

6

Turn

826 – 829

4

Helix

832 – 848

17

Helix

856 – 863

8

Helix

864 – 866

3

Helix

870 – 886

17

Helix

888 – 900

13

Helix

903 – 905

3

Helix

906 – 918

13

Turn

923 – 925

3

Helix

926 – 936

11

Helix

947 – 960

14

Helix

963 – 965

3

Helix

967 – 970

4

Turn

971 – 973

3

Beta strand

974 – 977

4

Helix

979 – 988

10

Helix

990 – 992

3

Helix

1001 – 1007

7

Turn

1009 – 1014

6

Beta strand

1015 – 1019

5

Helix

1021 – 1036

16

Helix

1038 – 1040

3

Helix

1042 – 1044

3

Helix

1045 – 1054

10

Helix

1060 – 1062

3

Beta strand

1063 – 1068

6

Beta strand

1071 – 1076

6

Helix

1079 – 1094

16

Beta strand

1098 – 1100

3

Helix

1102 – 1111

10

Helix

1117 – 1132

16

Helix

1136 – 1139

4

Turn

1140 – 1145

6

Helix

1146 – 1154

9

Helix

1163 – 1182

20

Beta strand

1190 – 1194

5

Helix

1200 – 1208

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: FE344558F72D79D8	FASTA	1,230	136,376
	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
	Isoform 2 [UniParc]. Checksum: 2045EBFCEE84468B	FASTA	1,062	117,889
	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 RQCCFNMLTT VKALTLIAGS PLKIDLRPVL 490 500 510 520 530 540 GEGVPILASF LRKNQRALKL GTLSALDILI KNYSDSLTAA MIDAVLDELP PLISESDMHV 550 560 570 580 590 600 SQMAISFLTT LAKVYPSSLS KISGSILNEL IGLVRSPLLQ GGALSAMLDF FQALVVTGTN 610 620 630 640 650 660 NLGYMDLLRM LTGPVYSQST ALTHKQSYYS IAKCVAALTR ACPKEGPAVV GQFIQDVKNS 670 680 690 700 710 720 RSTDSIRLLA LLSLGEVGHH IDLSGQLELK SVILEAFSSP SEEVKSAASY ALGSISVGNL 730 740 750 760 770 780 PEYLPFVLQE ITSQPKRQYL LLHSLKEIIS SASVVGLKPY VENIWALLLK HCECAEEGTR 790 800 810 820 830 840 NVVAECLGKL TLIDPETLLP RLKGYLISGS SYARSSVVTA VKFTISDHPQ PIDPLLKNCI 850 860 870 880 890 900 GDFLKTLEDP DLNVRRVALV TFNSAAHNKP SLIRDLLDTV LPHLYNETKV RKELIREVEM 910 920 930 940 950 960 GPFKHTVDDG LDIRKAAFEC MYTLLDSCLD RLDIFEFLNH VEDGLKDHYD IKMLTFLMLV 970 980 990 1000 1010 1020 RLSTLCPSAV LQRLDRLVEP LRATCTTKVK ANSVKQEFEK QDELKRSAMR AVAALLTIPE 1030 1040 1050 1060 AEKSPLMSEF QSQISSNPEL AAIFESIQKD SSSTNLESMD TS
	Isoform 3 [UniParc]. Checksum: 4EC2B75A93D82663	FASTA	403	45,539
	10 20 30 40 50 60 MADMLSRQGG LLVNFHPSIL TCLLPQLTSP RLAVRKRTII ALGHLVMSCG NIVFVDLIEH 70 80 90 100 110 120 LLSELSKNDS MSTTRTYIQC IAAISRQAGH RIGEYLEKII PLVVKFCNVD DDELREYCIQ 130 140 150 160 170 180 AFESFVRRCP KEVYPHVSTI INICLKYLTY DPNYNYDDED EDENAMDADG GDDDDQGSDD 190 200 210 220 230 240 EYSDDDDMSW KVRRAAAKCL DAVVSTRHEM LPEFYKTVSP ALISRFKERE ENVKADVFHA 250 260 270 280 290 300 YLSLLKQTRP VQSWLCDPDA MEQGETPLTM LQSQVPNIVK ALHKQMKEKS VKTRQCCFNM 310 320 330 340 350 360 LTELVNVLPG ALTQHIPVLV PGIIFSLNDK SSSSNLKIDA LSCLYVILCN HSPQVFHPHV 370 380 390 400 QALVPPVVAC VGDPFYKITS EALLVTQQLV KAHHMPEAQW LRL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, 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, 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, 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, MASS SPECTROMETRY. 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]	"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, MASS SPECTROMETRY.
[17]	"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.
[18]	"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.
[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]	"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.
[21]	"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 0:0-0(2013) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, REACTION MECHANISM.
[22]	"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.
[23]	"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.

IPI

IPI00100160.
IPI00604431.
IPI00915424.

PIR

T43441.

RefSeq

NP_060918.2. NM_018448.3.

UniGene

Hs.546407.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U6G	X-ray	3.10	C	1-1230	[»]
4A0C	X-ray	3.80	A/B	1-1230	[»]

ProteinModelPortal

Q86VP6.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31608N.

IntAct

Q86VP6. 12 interactions.

MINT

MINT-4999459.

PTM databases

PhosphoSite

Q86VP6.

Polymorphism databases

DMDM

67460541.

Proteomic databases

PaxDb

Q86VP6.

PRIDE

Q86VP6.

Protocols and materials databases

DNASU

55832.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000299218; ENSP00000299218; ENSG00000111530.
ENST00000544619; ENSP00000444089; ENSG00000111530.
ENST00000545606; ENSP00000442318; ENSG00000111530.

GeneID

55832.

KEGG

hsa:55832.

UCSC

uc001stn.2. human.
uc001sto.2. human.

Organism-specific databases

CTD

55832.

GeneCards

GC12P067663.

HGNC

HGNC:30688. CAND1.

MIM

607727. gene.

neXtProt

NX_Q86VP6.

PharmGKB

PA142672207.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG278162.

HOVERGEN

HBG053467.

InParanoid

Q86VP6.

OMA

MLTYLMT.

OrthoDB

EOG441Q9N.

PhylomeDB

Q86VP6.

Gene expression databases

ArrayExpress

Q86VP6.

Bgee

Q86VP6.

Genevestigator

Q86VP6.

GermOnline

ENSG00000111530. Homo sapiens.

Family and domain databases

Gene3D

1.25.10.10. 2 hits.

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013932. TATA-bd_TIP120.
[Graphical view]

Pfam

PF08623. TIP120. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50077. HEAT_REPEAT. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CAND1. human.

EvolutionaryTrace

Q86VP6.

GenomeRNAi

55832.

NextBio

61049.

SOURCE

Search...

Entry information

Entry name

CAND1_HUMAN

Accession

Primary (citable) accession number: Q86VP6
Secondary accession number(s): B2RAU3 , 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:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.