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S-phase kinase-associated protein 2 (Cyclin-A/CDK2-associated protein p45) (F-box protein Skp2) (F-box/LRR-repeat protein 1) (p45skp2)

 SKP2_HUMAN              Reviewed;         424 AA.
Q13309; A8K5E0; B4DJT4; Q8TDZ0; Q8TDZ1; Q9BV69;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
03-OCT-2003, sequence version 2.
13-FEB-2019, entry version 193.
RecName: Full=S-phase kinase-associated protein 2;
AltName: Full=Cyclin-A/CDK2-associated protein p45;
AltName: Full=F-box protein Skp2;
AltName: Full=F-box/LRR-repeat protein 1;
AltName: Full=p45skp2;
Name=SKP2; Synonyms=FBXL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 6-19;
31-58; 80-86 AND 365-372, AND INTERACTION WITH CYCLIN A-CDK2 COMPLEX.
PubMed=7553852; DOI=10.1016/0092-8674(95)90271-6;
Zhang H., Kobayashi R., Galaktionov K., Beach D.;
"p19Skp1 and p45Skp2 are essential elements of the cyclin A-CDK2 S
phase kinase.";
Cell 82:915-925(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver;
Yamaguchi T.;
"Human SKP2-like protein.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Prostatic carcinoma;
Kokontis J.M., Fukuchi J., Liao S.;
"Androgenic regulation of Skp2 in androgen-dependent and -independent
LNCaP human prostate tumor cells.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH RBL2, AND FUNCTION IN UBIQUITINATION OF RBL2.
PubMed=12435635; DOI=10.1101/gad.1011202;
Tedesco D., Lukas J., Reed S.I.;
"The pRb-related protein p130 is regulated by phosphorylation-
dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2).";
Genes Dev. 16:2946-2957(2002).
[9]
INTERACTION WITH ORC1, AND FUNCTION IN UBIQUITINATION OF ORC1.
PubMed=11931757; DOI=10.1016/S1097-2765(02)00467-7;
Mendez J., Zou-Yang X.H., Kim S.Y., Hidaka M., Tansey W.P.,
Stillman B.;
"Human origin recognition complex large subunit is degraded by
ubiquitin-mediated proteolysis after initiation of DNA replication.";
Mol. Cell 9:481-491(2002).
[10]
INTERACTION WITH CDT1, AND FUNCTION IN UBIQUITINATION OF CDT1.
PubMed=12840033; DOI=10.1074/jbc.C300251200;
Li X., Zhao Q., Liao R., Sun P., Wu X.;
"The SCF(Skp2) ubiquitin ligase complex interacts with the human
replication licensing factor Cdt1 and regulates Cdt1 degradation.";
J. Biol. Chem. 278:30854-30858(2003).
[11]
INTERACTION WITH MYC, AND FUNCTION IN UBIQUITINATION OF MYC.
PubMed=12769844; DOI=10.1016/S1097-2765(03)00193-X;
von der Lehr N., Johansson S., Wu S., Bahram F., Castell A.,
Cetinkaya C., Hydbring P., Weidung I., Nakayama K., Nakayama K.I.,
Soderberg O., Kerppola T.K., Larsson L.G.;
"The F-box protein Skp2 participates in c-Myc proteosomal degradation
and acts as a cofactor for c-Myc-regulated transcription.";
Mol. Cell 11:1189-1200(2003).
[12]
INTERACTION WITH UBP43, AND FUNCTION IN UBIQUITINATION OF UBP43.
PubMed=15342634; DOI=10.1074/jbc.M403189200;
Tokarz S., Berset C., La Rue J., Friedman K., Nakayama K.,
Nakayama K., Zhang D.E., Lanker S.;
"The ISG15 isopeptidase UBP43 is regulated by proteolysis via the
SCFSkp2 ubiquitin ligase.";
J. Biol. Chem. 279:46424-46430(2004).
[13]
FUNCTION IN UBIQUITINATION OF CDKN1A.
PubMed=16262255; DOI=10.1021/bi051071j;
Wang W., Nacusi L., Sheaff R.J., Liu X.;
"Ubiquitination of p21Cip1/WAF1 by SCFSkp2: substrate requirement and
ubiquitination site selection.";
Biochemistry 44:14553-14564(2005).
[14]
INTERACTION WITH RAG2, AND FUNCTION IN UBIQUITINATION OF RAG2.
PubMed=15949444; DOI=10.1016/j.molcel.2005.05.011;
Jiang H., Chang F.C., Ross A.E., Lee J., Nakayama K., Nakayama K.,
Desiderio S.;
"Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J
recombinase to the cell cycle.";
Mol. Cell 18:699-709(2005).
[15]
FUNCTION IN UBIQUITINATION OF CDK9.
PubMed=16103164; DOI=10.1128/JVI.79.17.11135-11141.2005;
Barboric M., Zhang F., Besenicar M., Plemenitas A., Peterlin B.M.;
"Ubiquitylation of Cdk9 by Skp2 facilitates optimal Tat
transactivation.";
J. Virol. 79:11135-11141(2005).
[16]
INTERACTION WITH FOXO1, AND FUNCTION IN UBIQUITINATION OF FOXO1.
PubMed=15668399; DOI=10.1073/pnas.0406789102;
Huang H., Regan K.M., Wang F., Wang D., Smith D.I., van Deursen J.M.,
Tindall D.J.;
"Skp2 inhibits FOXO1 in tumor suppression through ubiquitin-mediated
degradation.";
Proc. Natl. Acad. Sci. U.S.A. 102:1649-1654(2005).
[17]
INTERACTION WITH TOB1, AND FUNCTION IN UBIQUITINATION OF TOB1.
PubMed=16951159; DOI=10.1158/0008-5472.CAN-06-1603;
Hiramatsu Y., Kitagawa K., Suzuki T., Uchida C., Hattori T.,
Kikuchi H., Oda T., Hatakeyama S., Nakayama K.I., Yamamoto T.,
Konno H., Kitagawa M.;
"Degradation of Tob1 mediated by SCFSkp2-dependent ubiquitination.";
Cancer Res. 66:8477-8483(2006).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[19]
INTERACTION WITH ELF4, AND FUNCTION IN UBIQUITINATION OF ELF4.
PubMed=16581786; DOI=10.1128/MCB.26.8.3114-3123.2006;
Liu Y., Hedvat C.V., Mao S., Zhu X.H., Yao J., Nguyen H., Koff A.,
Nimer S.D.;
"The ETS protein MEF is regulated by phosphorylation-dependent
proteolysis via the protein-ubiquitin ligase SCFSkp2.";
Mol. Cell. Biol. 26:3114-3123(2006).
[20]
INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, AND INTERACTION WITH
TRIM21.
PubMed=16880511; DOI=10.1128/MCB.01630-05;
Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M.,
Krek W.;
"Regulation of p27 degradation and S-phase progression by Ro52 RING
finger protein.";
Mol. Cell. Biol. 26:5994-6004(2006).
[21]
INTERACTION WITH KMT2A/MLL1, AND FUNCTION IN UBIQUITINATION OF
KMT2A/MLL1.
PubMed=17908926; DOI=10.1101/gad.1574507;
Liu H., Cheng E.H., Hsieh J.J.;
"Bimodal degradation of MLL by SCFSkp2 and APCCdc20 assures cell cycle
execution: a critical regulatory circuit lost in leukemogenic MLL
fusions.";
Genes Dev. 21:2385-2398(2007).
[22]
INTERACTION WITH TAL1, AND FUNCTION IN UBIQUITINATION OF TAL1.
PubMed=17962192; DOI=10.1074/jbc.M704981200;
Nie L., Wu H., Sun X.H.;
"Ubiquitination and degradation of Tal1/SCL are induced by Notch
signaling and depend on Skp2 and CHIP.";
J. Biol. Chem. 283:684-692(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
DEUBIQUITINATION BY USP13.
PubMed=21571647; DOI=10.1073/pnas.1100028108;
Chen M., Gutierrez G.J., Ronai Z.A.;
"Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum
(ER) stress response to cell cycle control.";
Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[30]
FUNCTION, ACETYLATION AT LYS-68 AND LYS-71, NUCLEAR LOCALIZATION
SIGNAL, AND SUBCELLULAR LOCATION.
PubMed=22770219; DOI=10.1016/j.cell.2012.05.038;
Inuzuka H., Gao D., Finley L.W., Yang W., Wan L., Fukushima H.,
Chin Y.R., Zhai B., Shaik S., Lau A.W., Wang Z., Gygi S.P.,
Nakayama K., Teruya-Feldstein J., Toker A., Haigis M.C.,
Pandolfi P.P., Wei W.;
"Acetylation-dependent regulation of Skp2 function.";
Cell 150:179-193(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-72; SER-75 AND
SER-179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
FUNCTION, INTERACTION WITH IFI27 AND HEPATITIS C VIRUS NON-STRUCTURAL
PROTEIN NS5A, AND REGION.
PubMed=27194766; DOI=10.1128/JVI.00352-16;
Xue B., Yang D., Wang J., Xu Y., Wang X., Qin Y., Tian R., Chen S.,
Xie Q., Liu N., Zhu H.;
"ISG12a Restricts Hepatitis C Virus Infection through the
Ubiquitination-Dependent Degradation Pathway.";
J. Virol. 90:6832-6845(2016).
[33]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 89-424 IN COMPLEX WITH 1-147
OF SKP1, AND LEUCINE-RICH REPEATS.
PubMed=11099048; DOI=10.1038/35042620;
Schulman B.A., Carrano A.C., Jeffrey P.D., Bowen Z., Kinnucan E.R.E.,
Finnin M.S., Elledge S.J., Harper J.W., Pagano M., Pavletich N.P.;
"Insights into SCF ubiquitin ligases from the structure of the Skp1-
Skp2 complex.";
Nature 408:381-386(2000).
[34]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 97-137 IN COMPLEX WITH CUL1;
SKP1 AND RBX1, AND INTERACTION WITH CKS1.
PubMed=11961546; DOI=10.1038/416703a;
Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P.,
Chu C., Koepp D.M., Elledge S.J., Pagano M., Conaway R.C.,
Conaway J.W., Harper J.W., Pavletich N.P.;
"Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase
complex.";
Nature 416:703-709(2002).
-!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-
box protein) E3 ubiquitin-protein ligase complex which mediates
the ubiquitination and subsequent proteasomal degradation of
target proteins involved in cell cycle progression, signal
transduction and transcription. Specifically recognizes
phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S
transition. Degradation of CDKN1B/p27kip also requires CKS1.
Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9,
RAG2, FOXO1, UBP43, and probably MYC, TOB1 and TAL1. Degradation
of TAL1 also requires STUB1. Recognizes CDKN1A in association with
CCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destruction
of CDH1 in a CK1-Dependent Manner, thereby regulating cell
migration. {ECO:0000269|PubMed:11931757,
ECO:0000269|PubMed:12435635, ECO:0000269|PubMed:12769844,
ECO:0000269|PubMed:12840033, ECO:0000269|PubMed:15342634,
ECO:0000269|PubMed:15668399, ECO:0000269|PubMed:15949444,
ECO:0000269|PubMed:16103164, ECO:0000269|PubMed:16262255,
ECO:0000269|PubMed:16581786, ECO:0000269|PubMed:16951159,
ECO:0000269|PubMed:17908926, ECO:0000269|PubMed:17962192,
ECO:0000269|PubMed:22770219}.
-!- FUNCTION: Through the ubiquitin-mediated proteasomal degradation
of hepatitis C virus non-structural protein 5A, has an antiviral
activity towards that virus. {ECO:0000269|PubMed:27194766}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Part of a SCF(SKP2) complex consisting of CUL1, RBX1,
SKP1 and SKP2. Component of a SCF(SKP2)-like complex containing
CUL1, SKP1, TRIM21 and SKP2. Interacts directly with CUL1 and
SKP1. Interacts with CKS1. Interacts with the cyclin-A-CDK2
complex. Interacts with ORC1, phosphorylated CDT1, phosphorylated
RBL2, ELF4, phosphorylated RAG2, FOXO1, UBP43, MYC, TOB1, TAL1 and
KMT2A/MLL1. Interacts with TRIM21. Interacts with IFI27; promotes
the ubiquitin-mediated proteasomal degradation of NS5A
(PubMed:27194766). Interacts with hepatitis C virus/HCV non-
structural protein NS5A; promotes the ubiquitin-mediated
proteasomal degradation of NS5A (PubMed:27194766).
{ECO:0000269|PubMed:11099048, ECO:0000269|PubMed:11931757,
ECO:0000269|PubMed:11961546, ECO:0000269|PubMed:12435635,
ECO:0000269|PubMed:12769844, ECO:0000269|PubMed:12840033,
ECO:0000269|PubMed:15342634, ECO:0000269|PubMed:15668399,
ECO:0000269|PubMed:15949444, ECO:0000269|PubMed:16581786,
ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:16951159,
ECO:0000269|PubMed:17908926, ECO:0000269|PubMed:17962192,
ECO:0000269|PubMed:27194766, ECO:0000269|PubMed:7553852}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-456291, EBI-456291;
A5D8W4:CDH1; NbExp=2; IntAct=EBI-456291, EBI-7793316;
P09803:Cdh1 (xeno); NbExp=2; IntAct=EBI-456291, EBI-984420;
P38936:CDKN1A; NbExp=2; IntAct=EBI-456291, EBI-375077;
P46527:CDKN1B; NbExp=4; IntAct=EBI-456291, EBI-519280;
P61024:CKS1B; NbExp=6; IntAct=EBI-456291, EBI-456371;
Q13616:CUL1; NbExp=8; IntAct=EBI-456291, EBI-359390;
P28562:DUSP1; NbExp=3; IntAct=EBI-456291, EBI-975493;
Q09472:EP300; NbExp=3; IntAct=EBI-456291, EBI-447295;
Q9UM11:FZR1; NbExp=2; IntAct=EBI-456291, EBI-724997;
Q03164:KMT2A; NbExp=2; IntAct=EBI-15490084, EBI-591370;
P01106:MYC; NbExp=2; IntAct=EBI-456291, EBI-447544;
Q13415:ORC1; NbExp=2; IntAct=EBI-456291, EBI-374847;
P35232:PHB; NbExp=2; IntAct=EBI-7791408, EBI-354213;
P62877:RBX1; NbExp=3; IntAct=EBI-456291, EBI-398523;
Q9NTG7:SIRT3; NbExp=5; IntAct=EBI-456291, EBI-724621;
P63208:SKP1; NbExp=14; IntAct=EBI-456291, EBI-307486;
P63208-1:SKP1; NbExp=7; IntAct=EBI-15490084, EBI-307497;
Q4AE16:X (xeno); NbExp=3; IntAct=EBI-456291, EBI-7418293;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22770219}.
Nucleus {ECO:0000269|PubMed:22770219}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=SKP2-alpha;
IsoId=Q13309-1; Sequence=Displayed;
Name=2; Synonyms=SKP2-beta;
IsoId=Q13309-2; Sequence=VSP_008432;
Name=3;
IsoId=Q13309-4; Sequence=VSP_044931, VSP_044932;
Note=No experimental confirmation available.;
-!- PTM: Ubiquitinated by the APC/C complex, leading to its
degradation by the proteasome. Deubiquitinated by USP13.
{ECO:0000269|PubMed:21571647}.
-!- PTM: Acetylation at Lys-68 and Lys-71 increases stability through
impairment of APC/C-mediated proteolysis and promotes cytoplasmic
retention. Deacetylated by SIRT3. {ECO:0000269|PubMed:22770219}.
-!- SEQUENCE CAUTION:
Sequence=AAC50242.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB87202.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U33761; AAC50242.1; ALT_INIT; mRNA.
EMBL; AB050979; BAB87200.1; -; mRNA.
EMBL; AB050980; BAB87201.1; -; mRNA.
EMBL; AB050981; BAB87202.1; ALT_SEQ; mRNA.
EMBL; AY029177; AAK31593.1; -; mRNA.
EMBL; AK291255; BAF83944.1; -; mRNA.
EMBL; AK296223; BAG58946.1; -; mRNA.
EMBL; AC008942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471119; EAW55936.1; -; Genomic_DNA.
EMBL; BC001441; AAH01441.1; -; mRNA.
EMBL; BC007441; AAH07441.1; -; mRNA.
CCDS; CCDS3915.1; -. [Q13309-2]
CCDS; CCDS3916.1; -. [Q13309-1]
CCDS; CCDS58944.1; -. [Q13309-4]
PIR; I39171; I39171.
RefSeq; NP_001230049.1; NM_001243120.1. [Q13309-4]
RefSeq; NP_005974.2; NM_005983.3. [Q13309-1]
RefSeq; NP_116026.1; NM_032637.3. [Q13309-2]
UniGene; Hs.23348; -.
PDB; 1FQV; X-ray; 2.80 A; A/C/E/G/I/K/M/O=89-424.
PDB; 1FS1; X-ray; 1.80 A; A/C=89-141.
PDB; 1FS2; X-ray; 2.90 A; A/C=89-398.
PDB; 1LDK; X-ray; 3.10 A; E=97-137.
PDB; 2ASS; X-ray; 3.00 A; B=89-424.
PDB; 2AST; X-ray; 2.30 A; B=89-424.
PDBsum; 1FQV; -.
PDBsum; 1FS1; -.
PDBsum; 1FS2; -.
PDBsum; 1LDK; -.
PDBsum; 2ASS; -.
PDBsum; 2AST; -.
ProteinModelPortal; Q13309; -.
SMR; Q13309; -.
BioGrid; 112393; 191.
CORUM; Q13309; -.
DIP; DIP-17011N; -.
IntAct; Q13309; 57.
MINT; Q13309; -.
STRING; 9606.ENSP00000274255; -.
iPTMnet; Q13309; -.
PhosphoSitePlus; Q13309; -.
BioMuta; SKP2; -.
DMDM; 37537922; -.
EPD; Q13309; -.
jPOST; Q13309; -.
MaxQB; Q13309; -.
PaxDb; Q13309; -.
PeptideAtlas; Q13309; -.
PRIDE; Q13309; -.
ProteomicsDB; 59298; -.
ProteomicsDB; 59299; -. [Q13309-2]
TopDownProteomics; Q13309-1; -. [Q13309-1]
DNASU; 6502; -.
Ensembl; ENST00000274254; ENSP00000274254; ENSG00000145604. [Q13309-2]
Ensembl; ENST00000274255; ENSP00000274255; ENSG00000145604. [Q13309-1]
Ensembl; ENST00000620197; ENSP00000478031; ENSG00000145604. [Q13309-4]
GeneID; 6502; -.
KEGG; hsa:6502; -.
UCSC; uc003jkc.3; human. [Q13309-1]
CTD; 6502; -.
DisGeNET; 6502; -.
EuPathDB; HostDB:ENSG00000145604.15; -.
GeneCards; SKP2; -.
HGNC; HGNC:10901; SKP2.
HPA; CAB013491; -.
HPA; CAB013533; -.
HPA; HPA051196; -.
HPA; HPA054633; -.
MIM; 601436; gene.
neXtProt; NX_Q13309; -.
OpenTargets; ENSG00000145604; -.
PharmGKB; PA35801; -.
eggNOG; KOG2120; Eukaryota.
eggNOG; ENOG410Z2W2; LUCA.
GeneTree; ENSGT00390000007918; -.
HOGENOM; HOG000247037; -.
HOVERGEN; HBG047488; -.
InParanoid; Q13309; -.
KO; K03875; -.
OMA; EIWGIRC; -.
OrthoDB; 1333044at2759; -.
PhylomeDB; Q13309; -.
TreeFam; TF352582; -.
BioCyc; MetaCyc:ENSG00000145604-MONOMER; -.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; Q13309; -.
UniPathway; UPA00143; -.
ChiTaRS; SKP2; human.
EvolutionaryTrace; Q13309; -.
GeneWiki; SKP2; -.
GenomeRNAi; 6502; -.
PRO; PR:Q13309; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000145604; Expressed in 229 organ(s), highest expression level in oocyte.
ExpressionAtlas; Q13309; baseline and differential.
Genevisible; Q13309; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0008283; P:cell population proliferation; TAS:ProtInc.
GO; GO:0071460; P:cellular response to cell-matrix adhesion; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
GO; GO:1902916; P:positive regulation of protein polyubiquitination; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0070936; P:protein K48-linked ubiquitination; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0042981; P:regulation of apoptotic process; IDA:MGI.
GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
InterPro; IPR032675; LRR_dom_sf.
Pfam; PF12937; F-box-like; 1.
SMART; SM00256; FBOX; 1.
SMART; SM00367; LRR_CC; 5.
SUPFAM; SSF81383; SSF81383; 1.
PROSITE; PS50181; FBOX; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Antiviral defense;
Complete proteome; Cytoplasm; Direct protein sequencing;
Host-virus interaction; Immunity; Innate immunity;
Leucine-rich repeat; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 424 S-phase kinase-associated protein 2.
/FTId=PRO_0000119954.
DOMAIN 94 140 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 151 176 LRR 1. {ECO:0000269|PubMed:11099048}.
REPEAT 177 204 LRR 2. {ECO:0000269|PubMed:11099048}.
REPEAT 210 234 LRR 3. {ECO:0000269|PubMed:11099048}.
REPEAT 235 257 LRR 4. {ECO:0000269|PubMed:11099048}.
REPEAT 258 284 LRR 5. {ECO:0000269|PubMed:11099048}.
REPEAT 286 308 LRR 6. {ECO:0000269|PubMed:11099048}.
REPEAT 309 330 LRR 7. {ECO:0000269|PubMed:11099048}.
REPEAT 334 356 LRR 8. {ECO:0000269|PubMed:11099048}.
REPEAT 359 378 LRR 9. {ECO:0000269|PubMed:11099048}.
REPEAT 380 401 LRR 10. {ECO:0000269|PubMed:11099048}.
REGION 1 220 Mediates interaction with hepatitis C
virus non-structural protein NS5A.
{ECO:0000269|PubMed:27194766}.
REGION 402 424 Mediates interaction with IFI27.
{ECO:0000269|PubMed:27194766}.
MOTIF 67 73 Nuclear localization signal.
{ECO:0000269|PubMed:22770219}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 68 68 N6-acetyllysine; by p300/EP300.
{ECO:0000269|PubMed:22770219}.
MOD_RES 71 71 N6-acetyllysine; by p300/EP300.
{ECO:0000269|PubMed:22770219}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 169 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044931.
VAR_SEQ 180 224 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044932.
VAR_SEQ 355 424 ELGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTT
IARPTIGNKKNQEIWGIKCRLTLQKPSCL -> LVTRAGVR
IRLDSDIGCPQTYRTSKLKSSHKLFCQHVRVICIFVCDFYF
YRLVLKQ (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_008432.
VARIANT 85 85 P -> L (in dbSNP:rs3913486).
/FTId=VAR_016984.
VARIANT 87 87 L -> I (in dbSNP:rs3913487).
/FTId=VAR_016985.
CONFLICT 185 185 H -> D (in Ref. 1; AAC50242).
{ECO:0000305}.
CONFLICT 215 215 Missing (in Ref. 1; AAC50242).
{ECO:0000305}.
CONFLICT 238 238 S -> P (in Ref. 1; AAC50242).
{ECO:0000305}.
CONFLICT 241 241 S -> P (in Ref. 1; AAC50242).
{ECO:0000305}.
CONFLICT 244 247 SEFA -> PKFP (in Ref. 1; AAC50242).
{ECO:0000305}.
CONFLICT 251 251 L -> F (in Ref. 1; AAC50242).
{ECO:0000305}.
CONFLICT 256 256 S -> P (in Ref. 1; AAC50242).
{ECO:0000305}.
CONFLICT 268 268 D -> N (in Ref. 1; AAC50242).
{ECO:0000305}.
CONFLICT 285 285 I -> M (in Ref. 1; AAC50242).
{ECO:0000305}.
CONFLICT 319 319 D -> N (in Ref. 1; AAC50242).
{ECO:0000305}.
CONFLICT 332 332 F -> S (in Ref. 1; AAC50242).
{ECO:0000305}.
STRAND 97 100 {ECO:0000244|PDB:2AST}.
HELIX 102 109 {ECO:0000244|PDB:1FS1}.
HELIX 114 116 {ECO:0000244|PDB:1FS1}.
HELIX 117 121 {ECO:0000244|PDB:1FS1}.
HELIX 125 131 {ECO:0000244|PDB:1FS1}.
HELIX 134 136 {ECO:0000244|PDB:1FS1}.
STRAND 137 141 {ECO:0000244|PDB:2AST}.
HELIX 149 157 {ECO:0000244|PDB:2AST}.
STRAND 161 164 {ECO:0000244|PDB:2AST}.
STRAND 180 182 {ECO:0000244|PDB:1FS2}.
STRAND 185 187 {ECO:0000244|PDB:2AST}.
HELIX 195 202 {ECO:0000244|PDB:2AST}.
STRAND 209 212 {ECO:0000244|PDB:2AST}.
HELIX 220 226 {ECO:0000244|PDB:2AST}.
STRAND 233 236 {ECO:0000244|PDB:2AST}.
HELIX 245 254 {ECO:0000244|PDB:2AST}.
STRAND 260 262 {ECO:0000244|PDB:2AST}.
HELIX 271 280 {ECO:0000244|PDB:2AST}.
STRAND 287 289 {ECO:0000244|PDB:2AST}.
HELIX 294 296 {ECO:0000244|PDB:2AST}.
HELIX 299 308 {ECO:0000244|PDB:2AST}.
STRAND 313 316 {ECO:0000244|PDB:2AST}.
HELIX 325 333 {ECO:0000244|PDB:2AST}.
STRAND 339 341 {ECO:0000244|PDB:2AST}.
HELIX 350 358 {ECO:0000244|PDB:2AST}.
STRAND 364 366 {ECO:0000244|PDB:2AST}.
HELIX 376 382 {ECO:0000244|PDB:2AST}.
STRAND 386 389 {ECO:0000244|PDB:2AST}.
STRAND 402 404 {ECO:0000244|PDB:1FQV}.
STRAND 415 417 {ECO:0000244|PDB:2AST}.
SEQUENCE 424 AA; 47761 MW; F29B7C338A7A37E9 CRC64;
MHRKHLQEIP DLSSNVATSF TWGWDSSKTS ELLSGMGVSA LEKEEPDSEN IPQELLSNLG
HPESPPRKRL KSKGSDKDFV IVRRPKLNRE NFPGVSWDSL PDELLLGIFS CLCLPELLKV
SGVCKRWYRL ASDESLWQTL DLTGKNLHPD VTGRLLSQGV IAFRCPRSFM DQPLAEHFSP
FRVQHMDLSN SVIEVSTLHG ILSQCSKLQN LSLEGLRLSD PIVNTLAKNS NLVRLNLSGC
SGFSEFALQT LLSSCSRLDE LNLSWCFDFT EKHVQVAVAH VSETITQLNL SGYRKNLQKS
DLSTLVRRCP NLVHLDLSDS VMLKNDCFQE FFQLNYLQHL SLSRCYDIIP ETLLELGEIP
TLKTLQVFGI VPDGTLQLLK EALPHLQINC SHFTTIARPT IGNKKNQEIW GIKCRLTLQK
PSCL


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