SKP2_HUMAN
ID SKP2_HUMAN Reviewed; 424 AA.
AC Q13309; A8K5E0; B4DJT4; Q8TDZ0; Q8TDZ1; Q9BV69;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=S-phase kinase-associated protein 2;
DE AltName: Full=Cyclin-A/CDK2-associated protein p45;
DE AltName: Full=F-box protein Skp2;
DE AltName: Full=F-box/LRR-repeat protein 1;
DE AltName: Full=p45skp2;
GN Name=SKP2; Synonyms=FBXL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 6-19; 31-58;
RP 80-86 AND 365-372, AND INTERACTION WITH CYCLIN A-CDK2 COMPLEX.
RX PubMed=7553852; DOI=10.1016/0092-8674(95)90271-6;
RA Zhang H., Kobayashi R., Galaktionov K., Beach D.;
RT "p19Skp1 and p45Skp2 are essential elements of the cyclin A-CDK2 S phase
RT kinase.";
RL Cell 82:915-925(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver;
RA Yamaguchi T.;
RT "Human SKP2-like protein.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Prostatic carcinoma;
RA Kokontis J.M., Fukuchi J., Liao S.;
RT "Androgenic regulation of Skp2 in androgen-dependent and -independent LNCaP
RT human prostate tumor cells.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH RBL2, AND FUNCTION IN UBIQUITINATION OF RBL2.
RX PubMed=12435635; DOI=10.1101/gad.1011202;
RA Tedesco D., Lukas J., Reed S.I.;
RT "The pRb-related protein p130 is regulated by phosphorylation-dependent
RT proteolysis via the protein-ubiquitin ligase SCF(Skp2).";
RL Genes Dev. 16:2946-2957(2002).
RN [9]
RP INTERACTION WITH ORC1, AND FUNCTION IN UBIQUITINATION OF ORC1.
RX PubMed=11931757; DOI=10.1016/s1097-2765(02)00467-7;
RA Mendez J., Zou-Yang X.H., Kim S.Y., Hidaka M., Tansey W.P., Stillman B.;
RT "Human origin recognition complex large subunit is degraded by ubiquitin-
RT mediated proteolysis after initiation of DNA replication.";
RL Mol. Cell 9:481-491(2002).
RN [10]
RP INTERACTION WITH CDT1, AND FUNCTION IN UBIQUITINATION OF CDT1.
RX PubMed=12840033; DOI=10.1074/jbc.c300251200;
RA Li X., Zhao Q., Liao R., Sun P., Wu X.;
RT "The SCF(Skp2) ubiquitin ligase complex interacts with the human
RT replication licensing factor Cdt1 and regulates Cdt1 degradation.";
RL J. Biol. Chem. 278:30854-30858(2003).
RN [11]
RP INTERACTION WITH MYC, AND FUNCTION IN UBIQUITINATION OF MYC.
RX PubMed=12769844; DOI=10.1016/s1097-2765(03)00193-x;
RA von der Lehr N., Johansson S., Wu S., Bahram F., Castell A., Cetinkaya C.,
RA Hydbring P., Weidung I., Nakayama K., Nakayama K.I., Soderberg O.,
RA Kerppola T.K., Larsson L.G.;
RT "The F-box protein Skp2 participates in c-Myc proteosomal degradation and
RT acts as a cofactor for c-Myc-regulated transcription.";
RL Mol. Cell 11:1189-1200(2003).
RN [12]
RP INTERACTION WITH UBP43, AND FUNCTION IN UBIQUITINATION OF UBP43.
RX PubMed=15342634; DOI=10.1074/jbc.m403189200;
RA Tokarz S., Berset C., La Rue J., Friedman K., Nakayama K., Nakayama K.,
RA Zhang D.E., Lanker S.;
RT "The ISG15 isopeptidase UBP43 is regulated by proteolysis via the SCFSkp2
RT ubiquitin ligase.";
RL J. Biol. Chem. 279:46424-46430(2004).
RN [13]
RP FUNCTION IN UBIQUITINATION OF CDKN1A.
RX PubMed=16262255; DOI=10.1021/bi051071j;
RA Wang W., Nacusi L., Sheaff R.J., Liu X.;
RT "Ubiquitination of p21Cip1/WAF1 by SCFSkp2: substrate requirement and
RT ubiquitination site selection.";
RL Biochemistry 44:14553-14564(2005).
RN [14]
RP INTERACTION WITH RAG2, AND FUNCTION IN UBIQUITINATION OF RAG2.
RX PubMed=15949444; DOI=10.1016/j.molcel.2005.05.011;
RA Jiang H., Chang F.C., Ross A.E., Lee J., Nakayama K., Nakayama K.,
RA Desiderio S.;
RT "Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J
RT recombinase to the cell cycle.";
RL Mol. Cell 18:699-709(2005).
RN [15]
RP FUNCTION IN UBIQUITINATION OF CDK9.
RX PubMed=16103164; DOI=10.1128/jvi.79.17.11135-11141.2005;
RA Barboric M., Zhang F., Besenicar M., Plemenitas A., Peterlin B.M.;
RT "Ubiquitylation of Cdk9 by Skp2 facilitates optimal Tat transactivation.";
RL J. Virol. 79:11135-11141(2005).
RN [16]
RP INTERACTION WITH FOXO1, AND FUNCTION IN UBIQUITINATION OF FOXO1.
RX PubMed=15668399; DOI=10.1073/pnas.0406789102;
RA Huang H., Regan K.M., Wang F., Wang D., Smith D.I., van Deursen J.M.,
RA Tindall D.J.;
RT "Skp2 inhibits FOXO1 in tumor suppression through ubiquitin-mediated
RT degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1649-1654(2005).
RN [17]
RP INTERACTION WITH TOB1, AND FUNCTION IN UBIQUITINATION OF TOB1.
RX PubMed=16951159; DOI=10.1158/0008-5472.can-06-1603;
RA Hiramatsu Y., Kitagawa K., Suzuki T., Uchida C., Hattori T., Kikuchi H.,
RA Oda T., Hatakeyama S., Nakayama K.I., Yamamoto T., Konno H., Kitagawa M.;
RT "Degradation of Tob1 mediated by SCFSkp2-dependent ubiquitination.";
RL Cancer Res. 66:8477-8483(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [19]
RP INTERACTION WITH ELF4, AND FUNCTION IN UBIQUITINATION OF ELF4.
RX PubMed=16581786; DOI=10.1128/mcb.26.8.3114-3123.2006;
RA Liu Y., Hedvat C.V., Mao S., Zhu X.H., Yao J., Nguyen H., Koff A.,
RA Nimer S.D.;
RT "The ETS protein MEF is regulated by phosphorylation-dependent proteolysis
RT via the protein-ubiquitin ligase SCFSkp2.";
RL Mol. Cell. Biol. 26:3114-3123(2006).
RN [20]
RP INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, AND INTERACTION WITH TRIM21.
RX PubMed=16880511; DOI=10.1128/mcb.01630-05;
RA Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M.,
RA Krek W.;
RT "Regulation of p27 degradation and S-phase progression by Ro52 RING finger
RT protein.";
RL Mol. Cell. Biol. 26:5994-6004(2006).
RN [21]
RP INTERACTION WITH KMT2A/MLL1, AND FUNCTION IN UBIQUITINATION OF KMT2A/MLL1.
RX PubMed=17908926; DOI=10.1101/gad.1574507;
RA Liu H., Cheng E.H., Hsieh J.J.;
RT "Bimodal degradation of MLL by SCFSkp2 and APCCdc20 assures cell cycle
RT execution: a critical regulatory circuit lost in leukemogenic MLL
RT fusions.";
RL Genes Dev. 21:2385-2398(2007).
RN [22]
RP INTERACTION WITH TAL1, AND FUNCTION IN UBIQUITINATION OF TAL1.
RX PubMed=17962192; DOI=10.1074/jbc.m704981200;
RA Nie L., Wu H., Sun X.H.;
RT "Ubiquitination and degradation of Tal1/SCL are induced by Notch signaling
RT and depend on Skp2 and CHIP.";
RL J. Biol. Chem. 283:684-692(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP INTERACTION WITH ASB2.
RX PubMed=21119685; DOI=10.1038/cr.2010.165;
RA Nie L., Zhao Y., Wu W., Yang Y.Z., Wang H.C., Sun X.H.;
RT "Notch-induced Asb2 expression promotes protein ubiquitination by forming
RT non-canonical E3 ligase complexes.";
RL Cell Res. 21:754-769(2011).
RN [29]
RP DEUBIQUITINATION BY USP13.
RX PubMed=21571647; DOI=10.1073/pnas.1100028108;
RA Chen M., Gutierrez G.J., Ronai Z.A.;
RT "Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER)
RT stress response to cell cycle control.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP FUNCTION, ACETYLATION AT LYS-68 AND LYS-71, NUCLEAR LOCALIZATION SIGNAL,
RP AND SUBCELLULAR LOCATION.
RX PubMed=22770219; DOI=10.1016/j.cell.2012.05.038;
RA Inuzuka H., Gao D., Finley L.W., Yang W., Wan L., Fukushima H., Chin Y.R.,
RA Zhai B., Shaik S., Lau A.W., Wang Z., Gygi S.P., Nakayama K.,
RA Teruya-Feldstein J., Toker A., Haigis M.C., Pandolfi P.P., Wei W.;
RT "Acetylation-dependent regulation of Skp2 function.";
RL Cell 150:179-193(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-72; SER-75 AND
RP SER-179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP FUNCTION, INTERACTION WITH IFI27 AND HEPATITIS C VIRUS NON-STRUCTURAL
RP PROTEIN NS5A, AND REGION.
RX PubMed=27194766; DOI=10.1128/jvi.00352-16;
RA Xue B., Yang D., Wang J., Xu Y., Wang X., Qin Y., Tian R., Chen S., Xie Q.,
RA Liu N., Zhu H.;
RT "ISG12a Restricts Hepatitis C Virus Infection through the Ubiquitination-
RT Dependent Degradation Pathway.";
RL J. Virol. 90:6832-6845(2016).
RN [34]
RP FUNCTION IN UBIQUITINATION OF YTHDF2.
RX PubMed=32267835; DOI=10.1371/journal.pbio.3000664;
RA Fei Q., Zou Z., Roundtree I.A., Sun H.L., He C.;
RT "YTHDF2 promotes mitotic entry and is regulated by cell cycle mediators.";
RL PLoS Biol. 18:e3000664-e3000664(2020).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 89-424 IN COMPLEX WITH 1-147 OF
RP SKP1, AND LEUCINE-RICH REPEATS.
RX PubMed=11099048; DOI=10.1038/35042620;
RA Schulman B.A., Carrano A.C., Jeffrey P.D., Bowen Z., Kinnucan E.R.E.,
RA Finnin M.S., Elledge S.J., Harper J.W., Pagano M., Pavletich N.P.;
RT "Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2
RT complex.";
RL Nature 408:381-386(2000).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 97-137 IN COMPLEX WITH CUL1; SKP1
RP AND RBX1, AND INTERACTION WITH CKS1.
RX PubMed=11961546; DOI=10.1038/416703a;
RA Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P.,
RA Chu C., Koepp D.M., Elledge S.J., Pagano M., Conaway R.C., Conaway J.W.,
RA Harper J.W., Pavletich N.P.;
RT "Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex.";
RL Nature 416:703-709(2002).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins involved in cell cycle progression, signal transduction and
CC transcription (PubMed:11931757, PubMed:12435635, PubMed:12769844,
CC PubMed:12840033, PubMed:15342634, PubMed:15668399, PubMed:15949444,
CC PubMed:16103164, PubMed:16262255, PubMed:16581786, PubMed:16951159,
CC PubMed:17908926, PubMed:17962192, PubMed:22770219, PubMed:32267835).
CC Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in
CC regulation of G1/S transition (By similarity). Degradation of
CC CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1,
CC CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, YTHDF2, and probably
CC MYC, TOB1 and TAL1 (PubMed:11931757, PubMed:12435635, PubMed:12769844,
CC PubMed:12840033, PubMed:15342634, PubMed:15668399, PubMed:15949444,
CC PubMed:16103164, PubMed:17962192, PubMed:16581786, PubMed:16951159,
CC PubMed:17908926, PubMed:32267835). Degradation of TAL1 also requires
CC STUB1 (PubMed:17962192). Recognizes CDKN1A in association with CCNE1 or
CC CCNE2 and CDK2 (PubMed:16262255). Promotes ubiquitination and
CC destruction of CDH1 in a CK1-dependent manner, thereby regulating cell
CC migration (PubMed:22770219). {ECO:0000250|UniProtKB:Q9Z0Z3,
CC ECO:0000269|PubMed:11931757, ECO:0000269|PubMed:12435635,
CC ECO:0000269|PubMed:12769844, ECO:0000269|PubMed:12840033,
CC ECO:0000269|PubMed:15342634, ECO:0000269|PubMed:15668399,
CC ECO:0000269|PubMed:15949444, ECO:0000269|PubMed:16103164,
CC ECO:0000269|PubMed:16262255, ECO:0000269|PubMed:16581786,
CC ECO:0000269|PubMed:16951159, ECO:0000269|PubMed:17908926,
CC ECO:0000269|PubMed:17962192, ECO:0000269|PubMed:22770219,
CC ECO:0000269|PubMed:32267835}.
CC -!- FUNCTION: Through the ubiquitin-mediated proteasomal degradation of
CC hepatitis C virus non-structural protein 5A, has an antiviral activity
CC towards that virus. {ECO:0000269|PubMed:27194766}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF(SKP2) complex consisting of CUL1, RBX1, SKP1 and
CC SKP2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1,
CC TRIM21 and SKP2. Interacts directly with CUL1 and SKP1. Interacts with
CC CKS1. Interacts with ASB2 which is the substrate-recognition component
CC of a probable ECS E3 ubiquitin-protein ligase complex; ASB2 is likely
CC to bridge the formation of dimeric E3-ubiquitin-protein ligase
CC complexes composed of an ECS complex and an SCF(SKP2) complex
CC (PubMed:21119685). Interacts with the cyclin-A-CDK2 complex. Interacts
CC with ORC1, phosphorylated CDT1, phosphorylated RBL2, ELF4,
CC phosphorylated RAG2, FOXO1, UBP43, MYC, TOB1, TAL1 and KMT2A/MLL1.
CC Interacts with TRIM21. Interacts with cyclin-E (By similarity).
CC Interacts with IFI27; promotes the ubiquitin-mediated proteasomal
CC degradation of hepatitis C virus/HCV non-structural protein NS5A
CC (PubMed:27194766). Interacts with CARM1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z0Z3, ECO:0000269|PubMed:11099048,
CC ECO:0000269|PubMed:11931757, ECO:0000269|PubMed:11961546,
CC ECO:0000269|PubMed:12435635, ECO:0000269|PubMed:12769844,
CC ECO:0000269|PubMed:12840033, ECO:0000269|PubMed:15342634,
CC ECO:0000269|PubMed:15668399, ECO:0000269|PubMed:15949444,
CC ECO:0000269|PubMed:16581786, ECO:0000269|PubMed:16880511,
CC ECO:0000269|PubMed:16951159, ECO:0000269|PubMed:17908926,
CC ECO:0000269|PubMed:17962192, ECO:0000269|PubMed:21119685,
CC ECO:0000269|PubMed:27194766, ECO:0000269|PubMed:7553852}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus/HCV
CC non-structural protein NS5A; promotes the ubiquitin-mediated
CC proteasomal degradation of NS5A. {ECO:0000269|PubMed:27194766}.
CC -!- INTERACTION:
CC Q13309; A5D8W4: CDH1; NbExp=2; IntAct=EBI-456291, EBI-7793316;
CC Q13309; P38936: CDKN1A; NbExp=3; IntAct=EBI-456291, EBI-375077;
CC Q13309; P46527: CDKN1B; NbExp=4; IntAct=EBI-456291, EBI-519280;
CC Q13309; P61024: CKS1B; NbExp=7; IntAct=EBI-456291, EBI-456371;
CC Q13309; Q13616: CUL1; NbExp=15; IntAct=EBI-456291, EBI-359390;
CC Q13309; P28562: DUSP1; NbExp=3; IntAct=EBI-456291, EBI-975493;
CC Q13309; Q09472: EP300; NbExp=3; IntAct=EBI-456291, EBI-447295;
CC Q13309; Q9UM11: FZR1; NbExp=2; IntAct=EBI-456291, EBI-724997;
CC Q13309; P01106: MYC; NbExp=2; IntAct=EBI-456291, EBI-447544;
CC Q13309; Q13415: ORC1; NbExp=2; IntAct=EBI-456291, EBI-374847;
CC Q13309; P62877: RBX1; NbExp=3; IntAct=EBI-456291, EBI-398523;
CC Q13309; Q9NTG7: SIRT3; NbExp=5; IntAct=EBI-456291, EBI-724621;
CC Q13309; P63208: SKP1; NbExp=14; IntAct=EBI-456291, EBI-307486;
CC Q13309; Q13309: SKP2; NbExp=3; IntAct=EBI-456291, EBI-456291;
CC Q13309; P09803: Cdh1; Xeno; NbExp=2; IntAct=EBI-456291, EBI-984420;
CC Q13309; Q4AE16: X; Xeno; NbExp=3; IntAct=EBI-456291, EBI-7418293;
CC Q13309-1; Q03164: KMT2A; NbExp=2; IntAct=EBI-15490084, EBI-591370;
CC Q13309-1; P63208-1: SKP1; NbExp=7; IntAct=EBI-15490084, EBI-307497;
CC Q13309-2; P35232: PHB; NbExp=2; IntAct=EBI-7791408, EBI-354213;
CC Q13309-2; P63208: SKP1; NbExp=5; IntAct=EBI-7791408, EBI-307486;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22770219}. Nucleus
CC {ECO:0000269|PubMed:22770219}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SKP2-alpha;
CC IsoId=Q13309-1; Sequence=Displayed;
CC Name=2; Synonyms=SKP2-beta;
CC IsoId=Q13309-2; Sequence=VSP_008432;
CC Name=3;
CC IsoId=Q13309-4; Sequence=VSP_044931, VSP_044932;
CC -!- PTM: Ubiquitinated by the APC/C complex, leading to its degradation by
CC the proteasome. Deubiquitinated by USP13.
CC {ECO:0000269|PubMed:21571647}.
CC -!- PTM: Acetylation at Lys-68 and Lys-71 increases stability through
CC impairment of APC/C-mediated proteolysis and promotes cytoplasmic
CC retention. Deacetylated by SIRT3. {ECO:0000269|PubMed:22770219}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50242.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB87202.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; U33761; AAC50242.1; ALT_INIT; mRNA.
DR EMBL; AB050979; BAB87200.1; -; mRNA.
DR EMBL; AB050980; BAB87201.1; -; mRNA.
DR EMBL; AB050981; BAB87202.1; ALT_SEQ; mRNA.
DR EMBL; AY029177; AAK31593.1; -; mRNA.
DR EMBL; AK291255; BAF83944.1; -; mRNA.
DR EMBL; AK296223; BAG58946.1; -; mRNA.
DR EMBL; AC008942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471119; EAW55936.1; -; Genomic_DNA.
DR EMBL; BC001441; AAH01441.1; -; mRNA.
DR EMBL; BC007441; AAH07441.1; -; mRNA.
DR CCDS; CCDS3915.1; -. [Q13309-2]
DR CCDS; CCDS3916.1; -. [Q13309-1]
DR CCDS; CCDS58944.1; -. [Q13309-4]
DR PIR; I39171; I39171.
DR RefSeq; NP_001230049.1; NM_001243120.1. [Q13309-4]
DR RefSeq; NP_005974.2; NM_005983.3. [Q13309-1]
DR RefSeq; NP_116026.1; NM_032637.3. [Q13309-2]
DR PDB; 1FQV; X-ray; 2.80 A; A/C/E/G/I/K/M/O=89-424.
DR PDB; 1FS1; X-ray; 1.80 A; A/C=89-141.
DR PDB; 1FS2; X-ray; 2.90 A; A/C=89-398.
DR PDB; 1LDK; X-ray; 3.10 A; E=97-137.
DR PDB; 2ASS; X-ray; 3.00 A; B=89-424.
DR PDB; 2AST; X-ray; 2.30 A; B=89-424.
DR PDB; 7B5L; EM; 3.80 A; T=1-424.
DR PDB; 7B5M; EM; 3.91 A; T=1-424.
DR PDB; 7B5R; EM; 3.80 A; T=1-424.
DR PDBsum; 1FQV; -.
DR PDBsum; 1FS1; -.
DR PDBsum; 1FS2; -.
DR PDBsum; 1LDK; -.
DR PDBsum; 2ASS; -.
DR PDBsum; 2AST; -.
DR PDBsum; 7B5L; -.
DR PDBsum; 7B5M; -.
DR PDBsum; 7B5R; -.
DR AlphaFoldDB; Q13309; -.
DR SMR; Q13309; -.
DR BioGRID; 112393; 269.
DR CORUM; Q13309; -.
DR DIP; DIP-17011N; -.
DR IntAct; Q13309; 108.
DR MINT; Q13309; -.
DR STRING; 9606.ENSP00000274255; -.
DR iPTMnet; Q13309; -.
DR PhosphoSitePlus; Q13309; -.
DR BioMuta; SKP2; -.
DR DMDM; 37537922; -.
DR CPTAC; CPTAC-1267; -.
DR EPD; Q13309; -.
DR jPOST; Q13309; -.
DR MassIVE; Q13309; -.
DR MaxQB; Q13309; -.
DR PaxDb; Q13309; -.
DR PeptideAtlas; Q13309; -.
DR PRIDE; Q13309; -.
DR ProteomicsDB; 4402; -.
DR ProteomicsDB; 59298; -. [Q13309-1]
DR ProteomicsDB; 59299; -. [Q13309-2]
DR TopDownProteomics; Q13309-1; -. [Q13309-1]
DR Antibodypedia; 22921; 463 antibodies from 41 providers.
DR DNASU; 6502; -.
DR Ensembl; ENST00000274254.9; ENSP00000274254.5; ENSG00000145604.17. [Q13309-2]
DR Ensembl; ENST00000274255.11; ENSP00000274255.6; ENSG00000145604.17. [Q13309-1]
DR GeneID; 6502; -.
DR KEGG; hsa:6502; -.
DR MANE-Select; ENST00000274255.11; ENSP00000274255.6; NM_005983.4; NP_005974.2.
DR UCSC; uc003jkc.3; human. [Q13309-1]
DR CTD; 6502; -.
DR DisGeNET; 6502; -.
DR GeneCards; SKP2; -.
DR HGNC; HGNC:10901; SKP2.
DR HPA; ENSG00000145604; Tissue enhanced (placenta).
DR MIM; 601436; gene.
DR neXtProt; NX_Q13309; -.
DR OpenTargets; ENSG00000145604; -.
DR PharmGKB; PA35801; -.
DR VEuPathDB; HostDB:ENSG00000145604; -.
DR eggNOG; KOG2120; Eukaryota.
DR GeneTree; ENSGT00390000007918; -.
DR HOGENOM; CLU_1389772_0_0_1; -.
DR InParanoid; Q13309; -.
DR OMA; FVEELHF; -.
DR PhylomeDB; Q13309; -.
DR TreeFam; TF352582; -.
DR BioCyc; MetaCyc:ENSG00000145604-MON; -.
DR PathwayCommons; Q13309; -.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects.
DR Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q13309; -.
DR SIGNOR; Q13309; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 6502; 428 hits in 1116 CRISPR screens.
DR EvolutionaryTrace; Q13309; -.
DR GeneWiki; SKP2; -.
DR GenomeRNAi; 6502; -.
DR Pharos; Q13309; Tbio.
DR PRO; PR:Q13309; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q13309; protein.
DR Bgee; ENSG00000145604; Expressed in oocyte and 201 other tissues.
DR ExpressionAtlas; Q13309; baseline and differential.
DR Genevisible; Q13309; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 1.
DR IDEAL; IID00321; -.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 5.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antiviral defense;
KW Cytoplasm; Direct protein sequencing; Host-virus interaction; Immunity;
KW Innate immunity; Leucine-rich repeat; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..424
FT /note="S-phase kinase-associated protein 2"
FT /id="PRO_0000119954"
FT DOMAIN 94..140
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 151..176
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:11099048"
FT REPEAT 177..204
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:11099048"
FT REPEAT 210..234
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:11099048"
FT REPEAT 235..257
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:11099048"
FT REPEAT 258..284
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:11099048"
FT REPEAT 286..308
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:11099048"
FT REPEAT 309..330
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:11099048"
FT REPEAT 334..356
FT /note="LRR 8"
FT /evidence="ECO:0000269|PubMed:11099048"
FT REPEAT 359..378
FT /note="LRR 9"
FT /evidence="ECO:0000269|PubMed:11099048"
FT REPEAT 380..401
FT /note="LRR 10"
FT /evidence="ECO:0000269|PubMed:11099048"
FT REGION 1..220
FT /note="Mediates interaction with hepatitis C virus non-
FT structural protein NS5A"
FT /evidence="ECO:0000269|PubMed:27194766"
FT REGION 39..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..424
FT /note="Mediates interaction with IFI27"
FT /evidence="ECO:0000269|PubMed:27194766"
FT MOTIF 67..73
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:22770219"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 68
FT /note="N6-acetyllysine; by p300/EP300"
FT /evidence="ECO:0000269|PubMed:22770219"
FT MOD_RES 71
FT /note="N6-acetyllysine; by p300/EP300"
FT /evidence="ECO:0000269|PubMed:22770219"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..169
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044931"
FT VAR_SEQ 180..224
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044932"
FT VAR_SEQ 355..424
FT /note="ELGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKN
FT QEIWGIKCRLTLQKPSCL -> LVTRAGVRIRLDSDIGCPQTYRTSKLKSSHKLFCQHV
FT RVICIFVCDFYFYRLVLKQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_008432"
FT VARIANT 85
FT /note="P -> L (in dbSNP:rs3913486)"
FT /id="VAR_016984"
FT VARIANT 87
FT /note="L -> I (in dbSNP:rs3913487)"
FT /id="VAR_016985"
FT CONFLICT 185
FT /note="H -> D (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="Missing (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="S -> P (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="S -> P (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT CONFLICT 244..247
FT /note="SEFA -> PKFP (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="L -> F (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="S -> P (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="D -> N (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="I -> M (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="D -> N (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="F -> S (in Ref. 1; AAC50242)"
FT /evidence="ECO:0000305"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:1FS1"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1FS1"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:1FS1"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:1FS1"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1FS1"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1FS2"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 350..358
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2AST"
FT HELIX 376..382
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:2AST"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1FQV"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:2AST"
SQ 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
