Ubiquitin-conjugating enzyme E2 K Recombinant Protein | UBE2K recombinant protein

Recombinant Human Ubiquitin-conjugating enzyme E2 K

Cat. Num. AAA1265336

• Gene Names: UBE2K; LIG; HIP2; HYPG; UBC1; E2-25K
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Ubiquitin-conjugating enzyme E2 K; Recombinant Human Ubiquitin-conjugating enzyme E2 K; Huntingtin-interacting protein 2; HIP-2; Ubiquitin carrier protein; Ubiquitin-conjugating enzyme E2-25 kDa; Ubiquitin-conjugating enzyme E2(25K); Ubiquitin-conjugating enzyme E2-25K; Ubiquitin-protein ligase; UBE2K recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 2-200aa; Full Length
• Sequence: ANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN
• Sequence Length: 157

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for UBE2K recombinant protein

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1

Product Categories/Family for UBE2K recombinant protein

Neuroscience

References

Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme.Kalchman M.A., Graham R.K., Xia G., Koide H.B., Hodgson J.G., Graham K.C., Goldberg Y.P., Gietz R.D., Pickart C.M., Hayden M.R.J. Biol. Chem. 271:19385-19394(1996) Induction of ubiquitin-conjugating enzyme by aggregated low density lipoprotein in human macrophages and its implications for atherosclerosis.Kikuchi J., Furukawa Y., Kubo N., Tokura A., Hayashi N., Nakamura M., Matsuda M., Sakurabayashi I.Arterioscler. Thromb. Vasc. Biol. 20:128-134(2000) Regulation of macrophage-specific gene expression by degenerated lipoproteins.Furukawa Y., Kubo N., Kikuchi J., Tokura A., Fujita N., Sakurabayashi I.3.0.CO;2-9>Electrophoresis 21:338-346(2000) Full-length cDNA libraries and normalization.Li W.B., Gruber C., Jessee J., Polayes D. 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) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005)

NCBI and Uniprot Product Information

• NCBI GI #: 163660385
• NCBI GeneID: 3093
• NCBI Accession #: NP_001104582.1
• NCBI GenBank Nucleotide #: NM_001111112.1
• UniProt Accession #: P61086; O54806; P27924; Q16721; Q9CVV9; Q9Y2D3; A6NJC1; A8K5Y9; B2RDF8; C9JGP1
• Molecular Weight: 26.3 kDa
• NCBI Official Full Name: ubiquitin-conjugating enzyme E2 K isoform 2
• NCBI Official Synonym Full Names: ubiquitin conjugating enzyme E2K
• NCBI Official Symbol: UBE2K
• NCBI Official Synonym Symbols: LIG; HIP2; HYPG; UBC1; E2-25K
• NCBI Protein Information: ubiquitin-conjugating enzyme E2 K
• UniProt Protein Name: Ubiquitin-conjugating enzyme E2 K
• Protein Family: Ubiquitin-conjugating enzyme
• UniProt Gene Name: UBE2K
• UniProt Synonym Gene Names: HIP2; LIG; HIP-2; Ubiquitin-conjugating enzyme E2(25K); Ubiquitin-conjugating enzyme E2-25K
• UniProt Entry Name: UBE2K_HUMAN

NCBI Description

The protein encoded by this gene belongs to the ubiquitin-conjugating enzyme family. This protein interacts with RING finger proteins, and it can ubiquitinate huntingtin, the gene product for Huntington's disease. Known functions for this protein include a role in aggregate formation of expanded polyglutamine proteins and the suppression of apoptosis in polyglutamine diseases, a role in the dislocation of newly synthesized MHC class I heavy chains from the endoplasmic reticulum, and involvement in foam cell formation. Multiple transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

UBE2K: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein- dependent degradation of RB1. Interacts with RNF138/NARF. Interacts with BRCA1. By aggregated low-density lipoprotein. Expressed in all tissues tested, including spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, T-lymphocytes, monocytes, granulocytes and bone marrow mononuclear cells. Highly expressed in brain, with highest levels found in cortex and striatum and at lower levels in cerebellum and brainstem. Belongs to the ubiquitin-conjugating enzyme family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Ligase; Ubiquitin conjugating system; EC 6.3.2.19; Ubiquitin ligase

Chromosomal Location of Human Ortholog: 4p14

Cellular Component: cytoplasm; filopodium tip; nucleus

Molecular Function: ATP binding; protein binding; ubiquitin protein ligase binding; ubiquitin-protein ligase activity

Biological Process: proteasomal ubiquitin-dependent protein catabolic process; regulation of proteasomal ubiquitin-dependent protein catabolic process; ubiquitin-dependent protein catabolic process