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Protein

Cullin-2

Gene

CUL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. May serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity). The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF).By similarity

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • cell cycle arrest Source: ProtInc
  • cellular response to hypoxia Source: Reactome
  • G1/S transition of mitotic cell cycle Source: ProtInc
  • intrinsic apoptotic signaling pathway Source: ProtInc
  • negative regulation of cell proliferation Source: ProtInc
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: GO_Central
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-2
Short name:
CUL-2
Gene namesi
Name:CUL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:2552. CUL2.

Subcellular locationi

GO - Cellular componenti

  • Cul2-RING ubiquitin ligase complex Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi621 – 6211K → R: No effect on conjugation with NEDD8. 1 Publication
Mutagenesisi689 – 6891K → R: Loss of conjugation with NEDD8. 1 Publication
Mutagenesisi719 – 7191K → R: No effect on conjugation with NEDD8. 1 Publication

Organism-specific databases

PharmGKBiPA27048.

Polymorphism and mutation databases

BioMutaiCUL2.
DMDMi19863260.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 745745Cullin-2PRO_0000119790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei393 – 3931N6-acetyllysine1 Publication
Modified residuei661 – 6611Phosphothreonine1 Publication
Cross-linki689 – 689Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)

Post-translational modificationi

CBC(VHL) complex formation seems to promote neddylation. Deneddylated via its interaction with the COP9 signalosome (CSN) complex (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13617.
PaxDbiQ13617.
PRIDEiQ13617.

PTM databases

PhosphoSiteiQ13617.

Expressioni

Gene expression databases

BgeeiQ13617.
CleanExiHS_CUL2.
ExpressionAtlasiQ13617. baseline and differential.
GenevisibleiQ13617. HS.

Organism-specific databases

HPAiCAB002677.
HPA024578.

Interactioni

Subunit structurei

Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes formed of CUL2, Elongin BC (TCEB1 and TCEB2), RBX1 and a variable substrate-specific adapter. Component of the ECS(VHL) or CBC(VHL) complex containing VHL. Component of the ECS(MED8) complex with the probable substrate recognition component MED8. Component of the ECS(LRR1) complex with the probable substrate recognition component LRR1. Component of a probable ECS E3 ubiquitin-protein ligase complex containing CUL2, RBX1, TCEB1, TCEB2 and FEM1B. Part of an E3 ubiquitin-protein ligase complex including ZYG11B, CUL2 and Elongin BC. Part of an E3 ubiquitin-protein ligase complex including ZYG11BL, CUL2 and Elongin BC. Interacts with RBX1, RNF7, FEM1B and TIP120A/CAND1. Interacts with COPS2, and MED8. Interacts with human respiratory syncytial virus (HRSV) protein NS1. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 and CUL2. Interacts with KLHDC10; which may be an E3 ubiquitin ligase complex substrate recognition component.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAND1Q86VP63EBI-456179,EBI-456077
COMMD1Q8N6686EBI-456179,EBI-1550112
RBX1P628775EBI-456179,EBI-398523
TCEB1Q153696EBI-456179,EBI-301231
VHLP403379EBI-456179,EBI-301246
vifP125045EBI-456179,EBI-779991From a different organism.

Protein-protein interaction databases

BioGridi114031. 457 interactions.
DIPiDIP-31612N.
IntActiQ13617. 43 interactions.
MINTiMINT-1523339.
STRINGi9606.ENSP00000444856.

Structurei

Secondary structure

1
745
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2516Combined sources
Helixi32 – 4716Combined sources
Beta strandi49 – 513Combined sources
Helixi54 – 7724Combined sources
Helixi85 – 10420Combined sources
Helixi106 – 1127Combined sources
Helixi139 – 15618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WQOX-ray3.20D1-163[»]
ProteinModelPortaliQ13617.
SMRiQ13617. Positions 8-745.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5647.
GeneTreeiENSGT00760000119212.
HOGENOMiHOG000176713.
HOVERGENiHBG106177.
InParanoidiQ13617.
KOiK03870.
OrthoDBiEOG7X3QQG.
PhylomeDBiQ13617.
TreeFamiTF101152.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13617-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSLKPRVVDF DETWNKLLTT IKAVVMLEYV ERATWNDRFS DIYALCVAYP
60 70 80 90 100
EPLGERLYTE TKIFLENHVR HLHKRVLESE EQVLVMYHRY WEEYSKGADY
110 120 130 140 150
MDCLYRYLNT QFIKKNKLTE ADLQYGYGGV DMNEPLMEIG ELALDMWRKL
160 170 180 190 200
MVEPLQAILI RMLLREIKND RGGEDPNQKV IHGVINSFVH VEQYKKKFPL
210 220 230 240 250
KFYQEIFESP FLTETGEYYK QEASNLLQES NCSQYMEKVL GRLKDEEIRC
260 270 280 290 300
RKYLHPSSYT KVIHECQQRM VADHLQFLHA ECHNIIRQEK KNDMANMYVL
310 320 330 340 350
LRAVSTGLPH MIQELQNHIH DEGLRATSNL TQENMPTLFV ESVLEVHGKF
360 370 380 390 400
VQLINTVLNG DQHFMSALDK ALTSVVNYRE PKSVCKAPEL LAKYCDNLLK
410 420 430 440 450
KSAKGMTENE VEDRLTSFIT VFKYIDDKDV FQKFYARMLA KRLIHGLSMS
460 470 480 490 500
MDSEEAMINK LKQACGYEFT SKLHRMYTDM SVSADLNNKF NNFIKNQDTV
510 520 530 540 550
IDLGISFQIY VLQAGAWPLT QAPSSTFAIP QELEKSVQMF ELFYSQHFSG
560 570 580 590 600
RKLTWLHYLC TGEVKMNYLG KPYVAMVTTY QMAVLLAFNN SETVSYKELQ
610 620 630 640 650
DSTQMNEKEL TKTIKSLLDV KMINHDSEKE DIDAESSFSL NMNFSSKRTK
660 670 680 690 700
FKITTSMQKD TPQEMEQTRS AVDEDRKMYL QAAIVRIMKA RKVLRHNALI
710 720 730 740
QEVISQSRAR FNPSISMIKK CIEVLIDKQY IERSQASADE YSYVA
Length:745
Mass (Da):86,983
Last modified:August 14, 2001 - v2
Checksum:i30647248F671AB0E
GO
Isoform 2 (identifier: Q13617-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MYRVTWSTFWLRFQHYTCTM

Note: No experimental confirmation available.
Show »
Length:764
Mass (Da):89,492
Checksum:i11890883B1EA53A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201T → I in BAH13294 (PubMed:14702039).Curated
Sequence conflicti95 – 984SKGA → IRHE in AAC50545 (PubMed:8681378).Curated
Sequence conflicti681 – 6811Q → H in AAC50545 (PubMed:8681378).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti109 – 1091N → S.2 Publications
Corresponds to variant rs1131503 [ dbSNP | Ensembl ].
VAR_011374

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MYRVTWSTFWLRFQHYTCTM in isoform 2. 1 PublicationVSP_044498

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U83410 mRNA. Translation: AAC51190.1.
AF126404 mRNA. Translation: AAD23581.1.
AK095217 mRNA. Translation: BAG53007.1.
AK300491 mRNA. Translation: BAH13294.1.
AL392046 Genomic DNA. Translation: CAI13163.1.
CH471072 Genomic DNA. Translation: EAW85924.1.
CH471072 Genomic DNA. Translation: EAW85925.1.
CH471072 Genomic DNA. Translation: EAW85926.1.
CH471072 Genomic DNA. Translation: EAW85927.1.
CH471072 Genomic DNA. Translation: EAW85928.1.
BC009591 mRNA. Translation: AAH09591.1.
BC110901 mRNA. Translation: AAI10902.1.
U58088 mRNA. Translation: AAC50545.1.
CCDSiCCDS55709.1. [Q13617-2]
CCDS7179.1. [Q13617-1]
RefSeqiNP_001185706.1. NM_001198777.1. [Q13617-1]
NP_001185707.1. NM_001198778.1. [Q13617-2]
NP_001185708.1. NM_001198779.1.
NP_003582.2. NM_003591.3. [Q13617-1]
XP_011518048.1. XM_011519746.1. [Q13617-1]
XP_011518049.1. XM_011519747.1. [Q13617-1]
UniGeneiHs.82919.

Genome annotation databases

EnsembliENST00000374748; ENSP00000363880; ENSG00000108094.
ENST00000374749; ENSP00000363881; ENSG00000108094.
ENST00000374751; ENSP00000363883; ENSG00000108094.
ENST00000421317; ENSP00000414095; ENSG00000108094. [Q13617-2]
GeneIDi8453.
KEGGihsa:8453.
UCSCiuc001ixv.3. human. [Q13617-1]
uc010qer.2. human. [Q13617-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U83410 mRNA. Translation: AAC51190.1.
AF126404 mRNA. Translation: AAD23581.1.
AK095217 mRNA. Translation: BAG53007.1.
AK300491 mRNA. Translation: BAH13294.1.
AL392046 Genomic DNA. Translation: CAI13163.1.
CH471072 Genomic DNA. Translation: EAW85924.1.
CH471072 Genomic DNA. Translation: EAW85925.1.
CH471072 Genomic DNA. Translation: EAW85926.1.
CH471072 Genomic DNA. Translation: EAW85927.1.
CH471072 Genomic DNA. Translation: EAW85928.1.
BC009591 mRNA. Translation: AAH09591.1.
BC110901 mRNA. Translation: AAI10902.1.
U58088 mRNA. Translation: AAC50545.1.
CCDSiCCDS55709.1. [Q13617-2]
CCDS7179.1. [Q13617-1]
RefSeqiNP_001185706.1. NM_001198777.1. [Q13617-1]
NP_001185707.1. NM_001198778.1. [Q13617-2]
NP_001185708.1. NM_001198779.1.
NP_003582.2. NM_003591.3. [Q13617-1]
XP_011518048.1. XM_011519746.1. [Q13617-1]
XP_011518049.1. XM_011519747.1. [Q13617-1]
UniGeneiHs.82919.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WQOX-ray3.20D1-163[»]
ProteinModelPortaliQ13617.
SMRiQ13617. Positions 8-745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114031. 457 interactions.
DIPiDIP-31612N.
IntActiQ13617. 43 interactions.
MINTiMINT-1523339.
STRINGi9606.ENSP00000444856.

PTM databases

PhosphoSiteiQ13617.

Polymorphism and mutation databases

BioMutaiCUL2.
DMDMi19863260.

Proteomic databases

MaxQBiQ13617.
PaxDbiQ13617.
PRIDEiQ13617.

Protocols and materials databases

DNASUi8453.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374748; ENSP00000363880; ENSG00000108094.
ENST00000374749; ENSP00000363881; ENSG00000108094.
ENST00000374751; ENSP00000363883; ENSG00000108094.
ENST00000421317; ENSP00000414095; ENSG00000108094. [Q13617-2]
GeneIDi8453.
KEGGihsa:8453.
UCSCiuc001ixv.3. human. [Q13617-1]
uc010qer.2. human. [Q13617-2]

Organism-specific databases

CTDi8453.
GeneCardsiGC10M035338.
HGNCiHGNC:2552. CUL2.
HPAiCAB002677.
HPA024578.
MIMi603135. gene.
neXtProtiNX_Q13617.
PharmGKBiPA27048.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5647.
GeneTreeiENSGT00760000119212.
HOGENOMiHOG000176713.
HOVERGENiHBG106177.
InParanoidiQ13617.
KOiK03870.
OrthoDBiEOG7X3QQG.
PhylomeDBiQ13617.
TreeFamiTF101152.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiCUL2. human.
GeneWikiiCUL2.
GenomeRNAii8453.
NextBioi31634.
PROiQ13617.
SOURCEiSearch...

Gene expression databases

BgeeiQ13617.
CleanExiHS_CUL2.
ExpressionAtlasiQ13617. baseline and differential.
GenevisibleiQ13617. HS.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins."
    Pause A., Lee S., Worrel R., Chen D.Y.T., Burgess W.H., Linehan W.M., Klausner R.D.
    Proc. Natl. Acad. Sci. U.S.A. 94:2156-2161(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-109, IDENTIFICATION IN COMPLEX WITH VHL AND ELONGIN BC.
    Tissue: Kidney.
  2. "Identification of NEDD8-conjugation site in human cullin-2."
    Wada H., Yeh E.T.H., Kamitani T.
    Biochem. Biophys. Res. Commun. 257:100-105(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-109, MUTAGENESIS OF LYS-621; LYS-689 AND LYS-719, NEDDYLATION AT LYS-689.
    Tissue: Brain.
  3. "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 2).
    Tissue: Prostate.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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).
    Tissue: Brain and Skin.
  7. "cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family."
    Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.
    Cell 85:829-839(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 95-745.
  8. "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity."
    Ohta T., Michel J.J., Schottelius A.J., Xiong Y.
    Mol. Cell 3:535-541(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBX1 AND RNF7.
  9. "Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex."
    Kamura T., Sato S., Iwai K., Czyzyk-Krzeska M., Conaway R.C., Conaway J.W.
    Proc. Natl. Acad. Sci. U.S.A. 97:10430-10435(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN CBC(VHL) COMPLEX.
  10. "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase."
    Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E., Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 276:29748-29753(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH VHL; ELONGIN BC AND RBX1.
  11. "Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase."
    Brower C.S., Sato S., Tomomori-Sato C., Kamura T., Pause A., Stearman R., Klausner R.D., Malik S., Lane W.S., Sorokina I., Roeder R.G., Conaway J.W., Conaway R.C.
    Proc. Natl. Acad. Sci. U.S.A. 99:10353-10358(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH MED8.
  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: INTERACTION WITH TIP120A.
  13. "Covalent modification of all members of human cullin family proteins by NEDD8."
    Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N., Kato S., Tanaka K.
    Oncogene 18:6829-6834(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEDDYLATION.
  14. "VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases."
    Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C., Conaway J.W., Nakayama K.I.
    Genes Dev. 18:3055-3065(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRR1 AND FEM1B.
  15. "The Caenorhabditis elegans cell-cycle regulator ZYG-11 defines a conserved family of CUL-2 complex components."
    Vasudevan S., Starostina N.G., Kipreos E.T.
    EMBO Rep. 8:279-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH TCEB1 AND ZYG11B, IDENTIFICATION IN COMPLEX WITH TCEB1; TCEB2 AND CUL2.
  16. "Respiratory syncytial virus NS1 protein degrades STAT2 by using the Elongin-Cullin E3 ligase."
    Elliott J., Lynch O.T., Suessmuth Y., Qian P., Boyd C.R., Burrows J.F., Buick R., Stevenson N.J., Touzelet O., Gadina M., Power U.F., Johnston J.A.
    J. Virol. 81:3428-3436(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRSV VIRUS PROTEIN NS1.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "The Kelch repeat protein KLHDC10 regulates oxidative stress-induced ASK1 activation by suppressing PP5."
    Sekine Y., Hatanaka R., Watanabe T., Sono N., Iemura S., Natsume T., Kuranaga E., Miura M., Takeda K., Ichijo H.
    Mol. Cell 48:692-704(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTS WITH KLHDC10.
  21. Cited for: IDENTIFICATION IN A COMPLEX WITH LIMD1; EGLN1/PHD2; VHL AND TCEB2.

Entry informationi

Entry nameiCUL2_HUMAN
AccessioniPrimary (citable) accession number: Q13617
Secondary accession number(s): B3KT95
, B7Z6K8, D3DRY6, G3V1S2, O00200, Q5T2B6, Q9UNF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 14, 2001
Last modified: July 22, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.