Q13617 (CUL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cullin-2
Short name=CUL-2

Gene names

Name:

CUL2

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	745 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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).
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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 By similarity. 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 By similarity. Interacts with human respiratory syncytial virus (HRSV) protein NS1. Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, TCEB2 AND CUL2. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.20
Post-translational modification	CBC(VHL) complex formation seems to promote neddylation. Deneddylated via its interaction with the COP9 signalosome (CSN) complex By similarity.
Sequence similarities	Belongs to the cullin family.

Ontologies

Keywords
Biological process	Host-virus interaction Ubl conjugation pathway
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Traceable author statement Ref.7. Source: ProtInc cell cycle arrest Traceable author statement Ref.7. Source: ProtInc intrinsic apoptotic signaling pathway Traceable author statement Ref.7. Source: ProtInc negative regulation of cell proliferation Traceable author statement Ref.7. Source: ProtInc protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of transcription from RNA polymerase II promoter in response to hypoxia Traceable author statement. Source: Reactome ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Cul2-RING ubiquitin ligase complex Inferred from direct assay PubMed 17636018. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ubiquitin protein ligase binding Inferred from direct assay PubMed 17636018. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAND1	Q86VP6	3	EBI-456179,EBI-456077
vif	P12504	5	EBI-456179,EBI-779991	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13617-1)

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: Q13617-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 745	745	Cullin-2		PRO_0000119790
Amino acid modifications
	Modified residue	393	1	N6-acetyllysine Ref.18
	Modified residue	394	1	Phosphotyrosine By similarity
	Modified residue	661	1	Phosphothreonine Ref.17
	Cross-link	689		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) Ref.2
Natural variations
	Alternative sequence	1	1	M → MYRVTWSTFWLRFQHYTCTM in isoform 2.		VSP_044498
	Natural variant	109	1	N → S. Ref.1 Ref.2 Corresponds to variant rs1131503 [ dbSNP | Ensembl ].		VAR_011374
Experimental info
	Mutagenesis	621	1	K → R: No effect on conjugation with NEDD8. Ref.2
	Mutagenesis	689	1	K → R: Loss of conjugation with NEDD8. Ref.2
	Mutagenesis	719	1	K → R: No effect on conjugation with NEDD8. Ref.2
	Sequence conflict	20	1	T → I in BAH13294. Ref.3
	Sequence conflict	95 – 98	4	SKGA → IRHE in AAC50545. Ref.7
	Sequence conflict	681	1	Q → H in AAC50545. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: 30647248F671AB0E	FASTA	745	86,983
	10 20 30 40 50 60 MSLKPRVVDF DETWNKLLTT IKAVVMLEYV ERATWNDRFS DIYALCVAYP EPLGERLYTE 70 80 90 100 110 120 TKIFLENHVR HLHKRVLESE EQVLVMYHRY WEEYSKGADY MDCLYRYLNT QFIKKNKLTE 130 140 150 160 170 180 ADLQYGYGGV DMNEPLMEIG ELALDMWRKL MVEPLQAILI RMLLREIKND RGGEDPNQKV 190 200 210 220 230 240 IHGVINSFVH VEQYKKKFPL KFYQEIFESP FLTETGEYYK QEASNLLQES NCSQYMEKVL 250 260 270 280 290 300 GRLKDEEIRC RKYLHPSSYT KVIHECQQRM VADHLQFLHA ECHNIIRQEK KNDMANMYVL 310 320 330 340 350 360 LRAVSTGLPH MIQELQNHIH DEGLRATSNL TQENMPTLFV ESVLEVHGKF VQLINTVLNG 370 380 390 400 410 420 DQHFMSALDK ALTSVVNYRE PKSVCKAPEL LAKYCDNLLK KSAKGMTENE VEDRLTSFIT 430 440 450 460 470 480 VFKYIDDKDV FQKFYARMLA KRLIHGLSMS MDSEEAMINK LKQACGYEFT SKLHRMYTDM 490 500 510 520 530 540 SVSADLNNKF NNFIKNQDTV IDLGISFQIY VLQAGAWPLT QAPSSTFAIP QELEKSVQMF 550 560 570 580 590 600 ELFYSQHFSG RKLTWLHYLC TGEVKMNYLG KPYVAMVTTY QMAVLLAFNN SETVSYKELQ 610 620 630 640 650 660 DSTQMNEKEL TKTIKSLLDV KMINHDSEKE DIDAESSFSL NMNFSSKRTK FKITTSMQKD 670 680 690 700 710 720 TPQEMEQTRS AVDEDRKMYL QAAIVRIMKA RKVLRHNALI QEVISQSRAR FNPSISMIKK 730 740 CIEVLIDKQY IERSQASADE YSYVA
	Isoform 2 [UniParc]. Checksum: 11890883B1EA53A4	FASTA	764	89,492
	10 20 30 40 50 60 MYRVTWSTFW LRFQHYTCTM SLKPRVVDFD ETWNKLLTTI KAVVMLEYVE RATWNDRFSD 70 80 90 100 110 120 IYALCVAYPE PLGERLYTET KIFLENHVRH LHKRVLESEE QVLVMYHRYW EEYSKGADYM 130 140 150 160 170 180 DCLYRYLNTQ FIKKNKLTEA DLQYGYGGVD MNEPLMEIGE LALDMWRKLM VEPLQAILIR 190 200 210 220 230 240 MLLREIKNDR GGEDPNQKVI HGVINSFVHV EQYKKKFPLK FYQEIFESPF LTETGEYYKQ 250 260 270 280 290 300 EASNLLQESN CSQYMEKVLG RLKDEEIRCR KYLHPSSYTK VIHECQQRMV ADHLQFLHAE 310 320 330 340 350 360 CHNIIRQEKK NDMANMYVLL RAVSTGLPHM IQELQNHIHD EGLRATSNLT QENMPTLFVE 370 380 390 400 410 420 SVLEVHGKFV QLINTVLNGD QHFMSALDKA LTSVVNYREP KSVCKAPELL AKYCDNLLKK 430 440 450 460 470 480 SAKGMTENEV EDRLTSFITV FKYIDDKDVF QKFYARMLAK RLIHGLSMSM DSEEAMINKL 490 500 510 520 530 540 KQACGYEFTS KLHRMYTDMS VSADLNNKFN NFIKNQDTVI DLGISFQIYV LQAGAWPLTQ 550 560 570 580 590 600 APSSTFAIPQ ELEKSVQMFE LFYSQHFSGR KLTWLHYLCT GEVKMNYLGK PYVAMVTTYQ 610 620 630 640 650 660 MAVLLAFNNS ETVSYKELQD STQMNEKELT KTIKSLLDVK MINHDSEKED IDAESSFSLN 670 680 690 700 710 720 MNFSSKRTKF KITTSMQKDT PQEMEQTRSA VDEDRKMYLQ AAIVRIMKAR KVLRHNALIQ 730 740 750 760 EVISQSRARF NPSISMIKKC IEVLIDKQYI ERSQASADEY SYVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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 (SEP-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). 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]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-661, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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]	"The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity." Foxler D.E., Bridge K.S., James V., Webb T.M., Mee M., Wong S.C., Feng Y., Constantin-Teodosiu D., Petursdottir T.E., Bjornsson J., Ingvarsson S., Ratcliffe P.J., Longmore G.D., Sharp T.V. Nat. Cell Biol. 14:201-208(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH LIMD1; EGLN1/PHD2; VHL AND TCEB2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00014311. IPI00985090.
RefSeq	NP_001185706.1. NM_001198777.1. NP_001185707.1. NM_001198778.1. NP_001185708.1. NM_001198779.1. NP_003582.2. NM_003591.3.
UniGene	Hs.82919.
3D structure databases
ProteinModelPortal	Q13617.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31612N.
IntAct	Q13617. 29 interactions.
MINT	MINT-1523339.
STRING	9606.ENSP00000363880.
PTM databases
PhosphoSite	Q13617.
Polymorphism databases
DMDM	19863260.
Proteomic databases
PaxDb	Q13617.
PRIDE	Q13617.
Protocols and materials databases
DNASU	8453.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374748; ENSP00000363880; ENSG00000108094. ENST00000374749; ENSP00000363881; ENSG00000108094. ENST00000374751; ENSP00000363883; ENSG00000108094. ENST00000537177; ENSP00000444856; ENSG00000108094.
GeneID	8453.
KEGG	hsa:8453.
UCSC	uc001ixv.3. human.
Organism-specific databases
CTD	8453.
GeneCards	GC10M035338.
HGNC	HGNC:2552. CUL2.
HPA	CAB002677. HPA024578.
MIM	603135. gene.
neXtProt	NX_Q13617.
PharmGKB	PA27048.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5647.
HOVERGEN	HBG106177.
InParanoid	Q13617.
KO	K03870.
OMA	VMLDYVE.
OrthoDB	EOG4Z0B51.
PhylomeDB	Q13617.
Enzyme and pathway databases
Pathway_Interaction_DB	hif1apathway. Hypoxic and oxygen homeostasis regulation of HIF-1-alpha.
Reactome	REACT_120956. Cellular responses to stress. REACT_6900. Immune System.
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q13617.
Bgee	Q13617.
CleanEx	HS_CUL2.
Genevestigator	Q13617.
GermOnline	ENSG00000108094. Homo sapiens.
Family and domain databases
Gene3D	1.10.10.10. 2 hits.
InterPro	IPR016157. Cullin_CS. IPR016158. Cullin_homology. IPR001373. Cullin_N. IPR019559. Cullin_neddylation_domain. IPR016159. Cullin_repeat-like_dom. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF00888. Cullin. 1 hit. PF10557. Cullin_Nedd8. 1 hit. [Graphical view]
SMART	SM00182. CULLIN. 1 hit. SM00884. Cullin_Nedd8. 1 hit. [Graphical view]
SUPFAM	SSF75632. Cullin_homology. 1 hit. SSF74788. Cullin_repeat-like. 1 hit.
PROSITE	PS01256. CULLIN_1. 1 hit. PS50069. CULLIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CUL2. human.
GenomeRNAi	8453.
NextBio	31634.
SOURCE	Search...

Entry information

Entry name

CUL2_HUMAN

Accession

Primary (citable) accession number: Q13617
Secondary accession number(s): B3KT95 , B7Z6K8, D3DRY6, G3V1S2, O00200, Q5T2B6, Q9UNF9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	August 14, 2001
Last modified:	May 1, 2013
This is version 123 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.