SKP1_HUMAN
ID SKP1_HUMAN Reviewed; 163 AA.
AC P63208; D3DQ97; D3DQ98; P34991; Q8TAY2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=S-phase kinase-associated protein 1;
DE AltName: Full=Cyclin-A/CDK2-associated protein p19;
DE Short=p19A;
DE AltName: Full=Organ of Corti protein 2;
DE Short=OCP-2;
DE AltName: Full=Organ of Corti protein II;
DE Short=OCP-II;
DE AltName: Full=RNA polymerase II elongation factor-like protein;
DE AltName: Full=SIII;
DE AltName: Full=Transcription elongation factor B polypeptide 1-like;
DE AltName: Full=p19skp1;
GN Name=SKP1; Synonyms=EMC19, OCP2, SKP1A, TCEB1L;
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).
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] (ISOFORM 1).
RX PubMed=8530064; DOI=10.1006/geno.1995.1225;
RA Sowden J., Morrison K., Schofield J., Putt W., Edwards Y.;
RT "A novel cDNA with homology to an RNA polymerase II elongation factors maps
RT to human chromosome 5q31 (TCEB1L) and to mouse chromosome 11 (Tceb1l).";
RL Genomics 29:145-151(1995).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, Skin, and Uterus;
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 [5]
RP PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Erythrocyte;
RA Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., Pasquali C.,
RA Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., Balant L.,
RA Hochstrasser D.F.;
RL Submitted (FEB-1994) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, 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 [9]
RP FUNCTION IN UBIQUITINATION OF BCL2, AND IDENTIFICATION IN THE SCF(FBXO10)
RP COMPLEX.
RX PubMed=23431138; DOI=10.1073/pnas.1217271110;
RA Chiorazzi M., Rui L., Yang Y., Ceribelli M., Tishbi N., Maurer C.W.,
RA Ranuncolo S.M., Zhao H., Xu W., Chan W.C., Jaffe E.S., Gascoyne R.D.,
RA Campo E., Rosenwald A., Ott G., Delabie J., Rimsza L.M., Shaham S.,
RA Staudt L.M.;
RT "Related F-box proteins control cell death in Caenorhabditis elegans and
RT human lymphoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3943-3948(2013).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-163 (ISOFORM 1).
RC TISSUE=Inner ear;
RX PubMed=9031623; DOI=10.1016/s0378-1119(96)00590-2;
RA Liang Y., Chen H., Asher J.H. Jr., Chang C.-C., Friedman T.B.;
RT "Human inner ear OCP2 cDNA maps to 5q22-5q35.2 with related sequences on
RT chromosomes 4p16.2-4p14, 5p13-5q22, 7pter-q22, 10 and 12p13-12qter.";
RL Gene 184:163-167(1997).
RN [11]
RP INTERACTION WITH FBXW8, AND IDENTIFICATION IN SCF-LIKE COMPLEX.
RX PubMed=12481031; DOI=10.1073/pnas.252646399;
RA Dias D.C., Dolios G., Wang R., Pan Z.Q.;
RT "CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to form
RT an SCF-like complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002).
RN [12]
RP SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; UBE2D1; APC AND TBL1X.
RX PubMed=11389839; DOI=10.1016/s1097-2765(01)00242-8;
RA Matsuzawa S., Reed J.C.;
RT "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin
RT degradation linked to p53 responses.";
RL Mol. Cell 7:915-926(2001).
RN [13]
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 [14]
RP INTERACTION WITH FBXO44; FBXO17 AND FBXO27, AND IDENTIFICATION IN
RP SCF-COMPLEX.
RX PubMed=18203720; DOI=10.1074/jbc.m709508200;
RA Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.;
RT "Diversity in tissue expression, substrate binding, and SCF complex
RT formation for a lectin family of ubiquitin ligases.";
RL J. Biol. Chem. 283:12717-12729(2008).
RN [15]
RP IDENTIFICATION IN THE SCF(CCNF) COMPLEX.
RX PubMed=20596027; DOI=10.1038/nature09140;
RA D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L.,
RA Washburn M.P., Dynlacht B., Pagano M.;
RT "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through
RT CP110 degradation.";
RL Nature 466:138-142(2010).
RN [16]
RP FUNCTION IN UBIQUITINATION OF BCL6, AND IDENTIFICATION IN THE SCF(FBXO11)
RP COMPLEX.
RX PubMed=22113614; DOI=10.1038/nature10688;
RA Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C., di Celle P.F.,
RA Chapuy B., Shipp M., Chiarle R., Pagano M.;
RT "FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-
RT cell lymphomas.";
RL Nature 481:90-93(2012).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [19]
RP FUNCTION.
RX PubMed=25704143; DOI=10.1016/j.ejcb.2015.01.004;
RA Man X., Megraw T.L., Lim Y.P.;
RT "Cep68 can be regulated by Nek2 and SCF complex.";
RL Eur. J. Cell Biol. 94:162-172(2015).
RN [20]
RP INTERACTION WITH CEP68.
RX PubMed=25503564; DOI=10.1038/ncb3076;
RA Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V., Florens L.,
RA Washburn M.P., Pagano M.;
RT "Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM
RT to allow centriole separation, disengagement and licensing.";
RL Nat. Cell Biol. 17:31-43(2015).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP INTERACTION WITH NOTCH2.
RX PubMed=29149593; DOI=10.1016/j.molcel.2017.10.018;
RA Fukushima H., Shimizu K., Watahiki A., Hoshikawa S., Kosho T., Oba D.,
RA Sakano S., Arakaki M., Yamada A., Nagashima K., Okabe K., Fukumoto S.,
RA Jimi E., Bigas A., Nakayama K.I., Nakayama K., Aoki Y., Wei W., Inuzuka H.;
RT "NOTCH2 Hajdu-Cheney mutations escape SCFFBW7-dependent proteolysis to
RT promote osteoporosis.";
RL Mol. Cell 68:645-658(2017).
RN [23]
RP INTERACTION WITH VACCINIA VIRUS PROTEIN C9L (MICROBIAL INFECTION).
RX PubMed=29444943; DOI=10.1128/jvi.00053-18;
RA Liu R., Moss B.;
RT "Vaccinia Virus C9 Ankyrin Repeat/F-Box Protein Is a Newly Identified
RT Antagonist of the Type I Interferon-Induced Antiviral State.";
RL J. Virol. 92:0-0(2018).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF THE SKP1-SKP2 COMPLEX.
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 [25]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH CUL1; RBX1 AND
RP SKP2.
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).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH 176-606 OF BTRC AND
RP CTNNB1.
RX PubMed=12820959; DOI=10.1016/s1097-2765(03)00234-x;
RA Wu G., Xu G., Schulman B.A., Jeffrey P.D., Harper J.W., Pavletich N.P.;
RT "Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif
RT binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase.";
RL Mol. Cell 11:1445-1456(2003).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-159 IN COMPLEX WITH SKP2; CKS1B
RP AND CDKN1B PHOSPHOPEPTIDE, SUBUNIT, AND FUNCTION.
RX PubMed=16209941; DOI=10.1016/j.molcel.2005.09.003;
RA Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M.,
RA Pavletich N.P.;
RT "Structural basis of the Cks1-dependent recognition of p27(Kip1) by the
RT SCF(Skp2) ubiquitin ligase.";
RL Mol. Cell 20:9-19(2005).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FBXW7 AND CCNE1
RP PEPTIDE.
RX PubMed=17434132; DOI=10.1016/j.molcel.2007.02.022;
RA Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.;
RT "Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated
RT substrate recognition by SCF ubiquitin ligases.";
RL Mol. Cell 26:131-143(2007).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FBXO2.
RX PubMed=17389369; DOI=10.1073/pnas.0610312104;
RA Mizushima T., Yoshida Y., Kumanomidou T., Hasegawa Y., Suzuki A.,
RA Yamane T., Tanaka K.;
RT "Structural basis for the selection of glycosylated substrates by SCF(Fbs1)
RT ubiquitin ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5777-5781(2007).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FBXO4, AND FUNCTION.
RX PubMed=20181953; DOI=10.1074/jbc.m110.111518;
RA Li Y., Hao B.;
RT "Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4)
RT ubiquitin ligase.";
RL J. Biol. Chem. 285:13896-13906(2010).
RN [31] {ECO:0007744|PDB:5JH5}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 2-163, AND SUBUNIT.
RX PubMed=27568929; DOI=10.1016/j.str.2016.07.011;
RA Wong S.J., Gearhart M.D., Taylor A.B., Nanyes D.R., Ha D.J., Robinson A.K.,
RA Artigas J.A., Lee O.J., Demeler B., Hart P.J., Bardwell V.J., Kim C.A.;
RT "KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires
RT Cooperation between PCGF1 and BCORL1.";
RL Structure 24:1795-1801(2016).
RN [32] {ECO:0007744|PDB:5V4B}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH FBXW7, AND FUNCTION.
RX PubMed=28727686; DOI=10.1038/mp.2017.138;
RA Yalla K., Elliott C., Day J.P., Findlay J., Barratt S., Hughes Z.A.,
RA Wilson L., Whiteley E., Popiolek M., Li Y., Dunlop J., Killick R.,
RA Adams D.R., Brandon N.J., Houslay M.D., Hao B., Baillie G.S.;
RT "FBXW7 regulates DISC1 stability via the ubiquitin-proteosome system.";
RL Mol. Psychiatry 23:1278-1286(2018).
RN [33] {ECO:0007744|PDB:6BVA, ECO:0007744|PDB:6BYH, ECO:0007744|PDB:6C16}
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) IN COMPLEX WITH KDM2A; KDM2B AND
RP UBB, AND INTERACTION OF SKP1-KDM2A AND SKP1-KDM2B COMPLEXES WITH UBB.
RX PubMed=30033217; DOI=10.1016/j.str.2018.06.004;
RA Gorelik M., Manczyk N., Pavlenco A., Kurinov I., Sidhu S.S., Sicheri F.;
RT "A Structure-Based Strategy for Engineering Selective Ubiquitin Variant
RT Inhibitors of Skp1-Cul1-F-Box Ubiquitin Ligases.";
RL Structure 26:1226-1236.E3(2018).
CC -!- FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein)
CC ubiquitin ligase complex, which mediates the ubiquitination of proteins
CC involved in cell cycle progression, signal transduction and
CC transcription. In the SCF complex, serves as an adapter that links the
CC F-box protein to CUL1. The functional specificity of the SCF complex
CC depends on the F-box protein as substrate recognition component.
CC SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and
CC participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of
CC phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB,
CC NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5, CEP68 and probably NFKB2
CC (PubMed:25704143). SCF(SKP2) directs ubiquitination of phosphorylated
CC CDKN1B/p27kip and is involved in regulation of G1/S transition.
CC SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A,
CC RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs
CC ubiquitination of cyclin E, NOTCH1 released notch intracellular domain
CC (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1.
CC SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs
CC ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination
CC of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does
CC not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the
CC ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation
CC frees the associated NFKB1-RELA dimer to translocate into the nucleus
CC and to activate transcription. SCF(CCNF) directs ubiquitination of
CC CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and
CC CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2. SCF(FBXO10)
CC directs ubiquitination of BCL2. {ECO:0000269|PubMed:16209941,
CC ECO:0000269|PubMed:20181953, ECO:0000269|PubMed:22113614,
CC ECO:0000269|PubMed:23431138, ECO:0000269|PubMed:25704143,
CC ECO:0000269|PubMed:28727686}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with KDM2B, forming heterodimers (PubMed:27568929).
CC The KDM2B-SKP1 heterodimeric complex interacts with the PCGF1-BCORL
CC heterodimeric complex to form a homotetrameric polycomb repression
CC complex 1 (PRC1.1) (PubMed:27568929). Component of multiple SCF (SKP1-
CC CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1,
CC RBX1 and a variable F-box domain-containing protein as substrate-
CC specific subunit. Component of the SCF(FBXW11) complex containing
CC FBXW11. Component of the SCF(SKP2) complex containing SKP2, in which it
CC interacts directly with SKP1, SKP2 and RBX1. Component of the
CC SCF(FBXW2) complex containing FBXw2. Component of the SCF(FBXO32)
CC complex containing FBXO32. Component of the probable SCF(FBXO7) complex
CC containing FBXO7. Component of the SCF(FBXO10) complex containing
CC FBXO10. Component of the SCF(FBXO11) complex containing FBXO11.
CC Component of the SCF(FBXO25) complex containing FBXO25. Component of
CC the SCF(FBXO33) complex containing FBXO33. Component of the probable
CC SCF(FBXO4) complex containing FBXO4. Component of the SCF(FBXO44)
CC complex, composed of SKP1, CUL1 and FBXO44. Component of the SCF(BTRC)
CC complex, composed of SKP1, CUL1 and BTRC. This complex binds
CC phosphorylated NFKBIA. Part of a SCF complex consisting of CUL1, RBX1,
CC SKP1 and FBXO2. Component of a SCF(SKP2)-like complex containing CUL1,
CC SKP1, TRIM21 and SKP2. Component of the SCF(FBXO17) complex, composed
CC of SKP1, CUL1 and FBXO17. Component of the SCF(FBXO27) complex,
CC composed of SKP1, CUL1 and FBXO27. Component of the SCF(CCNF) complex
CC consisting of CUL1, RBX1, SKP1 and CCNF. Component of the SCF(FBXL3)
CC complex composed of CUL1, SKP1, RBX1 and FBXL3. Component of the
CC SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21. Component
CC of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Component of
CC the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and FBXW7
CC (PubMed:28727686). Interacts with CEP68 (PubMed:25503564). Interacts
CC with NOTCH2 (PubMed:29149593). Interacts with FBXW15 (By similarity).
CC The SKP1-KDM2A and SKP1-KDM2B complexes interact with UBB
CC (PubMed:30033217). {ECO:0000250|UniProtKB:Q9WTX5,
CC ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:12481031,
CC ECO:0000269|PubMed:12820959, ECO:0000269|PubMed:16209941,
CC ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:17389369,
CC ECO:0000269|PubMed:17434132, ECO:0000269|PubMed:18203720,
CC ECO:0000269|PubMed:20181953, ECO:0000269|PubMed:20596027,
CC ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23431138,
CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:27568929,
CC ECO:0000269|PubMed:28727686, ECO:0000269|PubMed:29149593,
CC ECO:0000269|PubMed:30033217}.
CC -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein
CC C9L. {ECO:0000269|PubMed:29444943}.
CC -!- INTERACTION:
CC P63208; Q96IX9: ANKRD36BP1; NbExp=3; IntAct=EBI-307486, EBI-744859;
CC P63208; Q96GX9: APIP; NbExp=3; IntAct=EBI-307486, EBI-359248;
CC P63208; P54253: ATXN1; NbExp=6; IntAct=EBI-307486, EBI-930964;
CC P63208; Q9Y297: BTRC; NbExp=17; IntAct=EBI-307486, EBI-307461;
CC P63208; P41002: CCNF; NbExp=6; IntAct=EBI-307486, EBI-1207574;
CC P63208; P38936: CDKN1A; NbExp=3; IntAct=EBI-307486, EBI-375077;
CC P63208; Q13616: CUL1; NbExp=17; IntAct=EBI-307486, EBI-359390;
CC P63208; Q9NXK8: FBXL12; NbExp=7; IntAct=EBI-307486, EBI-719790;
CC P63208; Q8N1E6: FBXL14; NbExp=5; IntAct=EBI-307486, EBI-6425532;
CC P63208; Q9UKC9: FBXL2; NbExp=6; IntAct=EBI-307486, EBI-724253;
CC P63208; Q96IG2: FBXL20; NbExp=4; IntAct=EBI-307486, EBI-8835647;
CC P63208; Q6P050: FBXL22; NbExp=3; IntAct=EBI-307486, EBI-24224082;
CC P63208; Q9UKA1: FBXL5; NbExp=12; IntAct=EBI-307486, EBI-2692340;
CC P63208; Q96CD0: FBXL8; NbExp=14; IntAct=EBI-307486, EBI-2321097;
CC P63208; Q86XK2: FBXO11; NbExp=8; IntAct=EBI-307486, EBI-1047804;
CC P63208; Q96EF6: FBXO17; NbExp=16; IntAct=EBI-307486, EBI-2510157;
CC P63208; Q9UK22: FBXO2; NbExp=11; IntAct=EBI-307486, EBI-4287196;
CC P63208; Q8NEZ5: FBXO22; NbExp=7; IntAct=EBI-307486, EBI-2510137;
CC P63208; Q8TCJ0-3: FBXO25; NbExp=4; IntAct=EBI-307486, EBI-6262578;
CC P63208; Q8NI29: FBXO27; NbExp=3; IntAct=EBI-307486, EBI-6425694;
CC P63208; Q9NVF7: FBXO28; NbExp=11; IntAct=EBI-307486, EBI-740282;
CC P63208; Q9UK99: FBXO3; NbExp=9; IntAct=EBI-307486, EBI-2509901;
CC P63208; Q7Z6M2: FBXO33; NbExp=2; IntAct=EBI-307486, EBI-8555452;
CC P63208; Q9UKT5: FBXO4; NbExp=16; IntAct=EBI-307486, EBI-960409;
CC P63208; Q4G163: FBXO43; NbExp=3; IntAct=EBI-307486, EBI-12053217;
CC P63208; Q9H4M3: FBXO44; NbExp=5; IntAct=EBI-307486, EBI-2322644;
CC P63208; Q9H4M3-2: FBXO44; NbExp=6; IntAct=EBI-307486, EBI-12104696;
CC P63208; Q6PJ61: FBXO46; NbExp=4; IntAct=EBI-307486, EBI-2322982;
CC P63208; Q5FWF7: FBXO48; NbExp=5; IntAct=EBI-307486, EBI-11961122;
CC P63208; Q9UKT4: FBXO5; NbExp=5; IntAct=EBI-307486, EBI-852298;
CC P63208; Q9NRD1: FBXO6; NbExp=8; IntAct=EBI-307486, EBI-3938499;
CC P63208; Q9Y3I1: FBXO7; NbExp=8; IntAct=EBI-307486, EBI-1161222;
CC P63208; Q9UK97: FBXO9; NbExp=2; IntAct=EBI-307486, EBI-2869927;
CC P63208; Q9UK97-2: FBXO9; NbExp=3; IntAct=EBI-307486, EBI-11023199;
CC P63208; Q9UKB1: FBXW11; NbExp=10; IntAct=EBI-307486, EBI-355189;
CC P63208; Q9UKT8: FBXW2; NbExp=4; IntAct=EBI-307486, EBI-914727;
CC P63208; P57775: FBXW4; NbExp=2; IntAct=EBI-307486, EBI-2372268;
CC P63208; Q969U6: FBXW5; NbExp=4; IntAct=EBI-307486, EBI-741068;
CC P63208; Q969H0: FBXW7; NbExp=11; IntAct=EBI-307486, EBI-359574;
CC P63208; Q8N3Y1: FBXW8; NbExp=2; IntAct=EBI-307486, EBI-914770;
CC P63208; Q5XUX1: FBXW9; NbExp=4; IntAct=EBI-307486, EBI-2322729;
CC P63208; Q7L273: KCTD9; NbExp=3; IntAct=EBI-307486, EBI-4397613;
CC P63208; Q9Y2K7: KDM2A; NbExp=3; IntAct=EBI-307486, EBI-765758;
CC P63208; Q8NHM5: KDM2B; NbExp=3; IntAct=EBI-307486, EBI-3955564;
CC P63208; P25791: LMO2; NbExp=3; IntAct=EBI-307486, EBI-739696;
CC P63208; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-307486, EBI-16439278;
CC P63208; Q9ULD2-3: MTUS1; NbExp=3; IntAct=EBI-307486, EBI-18051665;
CC P63208; Q14901: MYC; NbExp=2; IntAct=EBI-307486, EBI-7982457;
CC P63208; P62136: PPP1CA; NbExp=3; IntAct=EBI-307486, EBI-357253;
CC P63208; Q13309: SKP2; NbExp=14; IntAct=EBI-307486, EBI-456291;
CC P63208; Q13309-2: SKP2; NbExp=5; IntAct=EBI-307486, EBI-7791408;
CC P63208; Q9Y2Z0-2: SUGT1; NbExp=2; IntAct=EBI-307486, EBI-10768076;
CC P63208; A0A0B4J1Y2: TTC21A; NbExp=3; IntAct=EBI-307486, EBI-10220701;
CC P63208; Q8N5M4: TTC9C; NbExp=10; IntAct=EBI-307486, EBI-2851213;
CC P63208; Q8BFZ4: Fbxl21; Xeno; NbExp=3; IntAct=EBI-307486, EBI-6898235;
CC P63208; Q8C4V4: Fbxl3; Xeno; NbExp=3; IntAct=EBI-307486, EBI-1266589;
CC P63208-1; P41002: CCNF; NbExp=6; IntAct=EBI-307497, EBI-1207574;
CC P63208-1; Q86XK2: FBXO11; NbExp=5; IntAct=EBI-307497, EBI-1047804;
CC P63208-1; Q969U6-1: FBXW5; NbExp=3; IntAct=EBI-307497, EBI-16031873;
CC P63208-1; Q969H0: FBXW7; NbExp=2; IntAct=EBI-307497, EBI-359574;
CC P63208-1; Q13503: MED21; NbExp=5; IntAct=EBI-307497, EBI-394678;
CC P63208-1; Q13309-1: SKP2; NbExp=7; IntAct=EBI-307497, EBI-15490084;
CC P63208-1; Q80UW2: Fbxo2; Xeno; NbExp=4; IntAct=EBI-307497, EBI-2314714;
CC P63208-1; Q6TVJ2; Xeno; NbExp=2; IntAct=EBI-307497, EBI-15718764;
CC P63208-1; Q6TVJ4; Xeno; NbExp=2; IntAct=EBI-307497, EBI-15718558;
CC P63208-1; Q6TVJ7; Xeno; NbExp=2; IntAct=EBI-307497, EBI-15718586;
CC P63208-1; Q6TVW2; Xeno; NbExp=5; IntAct=EBI-307497, EBI-15718527;
CC P63208-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25930963, EBI-5235340;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63208-1, P34991-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P63208-2, P34991-2;
CC Sequence=VSP_007555;
CC -!- PTM: Undergoes autophagy-mediated degradation in the liver in a time-
CC dependent manner. {ECO:0000250|UniProtKB:Q9WTX5}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR EMBL; U33760; AAC50241.1; -; mRNA.
DR EMBL; Z47087; CAA87392.1; -; mRNA.
DR EMBL; CH471062; EAW62270.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62271.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62272.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62276.1; -; Genomic_DNA.
DR EMBL; BC009839; AAH09839.1; -; mRNA.
DR EMBL; BC020798; AAH20798.1; -; mRNA.
DR EMBL; BC025673; AAH25673.1; -; mRNA.
DR EMBL; BC065730; AAH65730.1; -; mRNA.
DR EMBL; U37558; AAA79202.1; -; mRNA.
DR CCDS; CCDS4171.1; -.
DR CCDS; CCDS4172.1; -. [P63208-2]
DR PIR; I39170; I39170.
DR RefSeq; NP_008861.2; NM_006930.3. [P63208-2]
DR RefSeq; NP_733779.1; NM_170679.2. [P63208-1]
DR PDB; 1FQV; X-ray; 2.80 A; B/D/F/H/J/L/N/P=1-163.
DR PDB; 1FS1; X-ray; 1.80 A; B/D=1-147.
DR PDB; 1FS2; X-ray; 2.90 A; B/D=1-147.
DR PDB; 1LDK; X-ray; 3.10 A; D=2-140.
DR PDB; 1P22; X-ray; 2.95 A; B=1-163.
DR PDB; 2ASS; X-ray; 3.00 A; A=2-160.
DR PDB; 2AST; X-ray; 2.30 A; A=2-160.
DR PDB; 2E31; X-ray; 2.40 A; B=1-163.
DR PDB; 2E32; X-ray; 3.52 A; B/D=1-163.
DR PDB; 2OVP; X-ray; 2.90 A; A=1-163.
DR PDB; 2OVQ; X-ray; 2.60 A; A=1-163.
DR PDB; 2OVR; X-ray; 2.50 A; A=1-163.
DR PDB; 3L2O; X-ray; 2.80 A; A=1-69, A=82-163.
DR PDB; 3WSO; X-ray; 2.60 A; B=1-163.
DR PDB; 4I6J; X-ray; 2.70 A; C=1-163.
DR PDB; 5IBK; X-ray; 2.50 A; A/D=1-69, A/D=82-163.
DR PDB; 5JH5; X-ray; 2.55 A; B=2-163.
DR PDB; 5K35; X-ray; 2.85 A; B=1-163.
DR PDB; 5V4B; X-ray; 2.60 A; A=1-163.
DR PDB; 5VZT; X-ray; 2.70 A; A/C=1-163.
DR PDB; 5VZU; X-ray; 2.70 A; A/C=1-163.
DR PDB; 5XYL; NMR; -; A=1-163.
DR PDB; 6BVA; X-ray; 2.66 A; C/D=1-163.
DR PDB; 6BYH; X-ray; 2.61 A; A/B/G=1-163.
DR PDB; 6C16; X-ray; 3.27 A; A/B=1-163.
DR PDB; 6M90; X-ray; 2.05 A; B=2-163.
DR PDB; 6M91; X-ray; 2.40 A; B=2-163.
DR PDB; 6M92; X-ray; 2.35 A; B=2-163.
DR PDB; 6M93; X-ray; 2.50 A; B=2-163.
DR PDB; 6M94; X-ray; 2.70 A; B=2-163.
DR PDB; 6O60; X-ray; 2.50 A; D=1-163.
DR PDB; 6TTU; EM; 3.70 A; S=1-163.
DR PDB; 6VCD; EM; 3.00 A; C=1-163.
DR PDB; 6W66; X-ray; 3.21 A; A=1-163.
DR PDB; 6WCQ; EM; 8.50 A; A=1-163.
DR PDB; 6WNX; X-ray; 2.50 A; B/E/H=1-163.
DR PDB; 7B5L; EM; 3.80 A; S=1-163.
DR PDB; 7B5M; EM; 3.91 A; S=1-163.
DR PDB; 7B5R; EM; 3.80 A; S=1-163.
DR PDB; 7T1Y; X-ray; 2.55 A; A=1-163.
DR PDB; 7T1Z; X-ray; 2.77 A; A=1-69, A=89-163.
DR PDBsum; 1FQV; -.
DR PDBsum; 1FS1; -.
DR PDBsum; 1FS2; -.
DR PDBsum; 1LDK; -.
DR PDBsum; 1P22; -.
DR PDBsum; 2ASS; -.
DR PDBsum; 2AST; -.
DR PDBsum; 2E31; -.
DR PDBsum; 2E32; -.
DR PDBsum; 2OVP; -.
DR PDBsum; 2OVQ; -.
DR PDBsum; 2OVR; -.
DR PDBsum; 3L2O; -.
DR PDBsum; 3WSO; -.
DR PDBsum; 4I6J; -.
DR PDBsum; 5IBK; -.
DR PDBsum; 5JH5; -.
DR PDBsum; 5K35; -.
DR PDBsum; 5V4B; -.
DR PDBsum; 5VZT; -.
DR PDBsum; 5VZU; -.
DR PDBsum; 5XYL; -.
DR PDBsum; 6BVA; -.
DR PDBsum; 6BYH; -.
DR PDBsum; 6C16; -.
DR PDBsum; 6M90; -.
DR PDBsum; 6M91; -.
DR PDBsum; 6M92; -.
DR PDBsum; 6M93; -.
DR PDBsum; 6M94; -.
DR PDBsum; 6O60; -.
DR PDBsum; 6TTU; -.
DR PDBsum; 6VCD; -.
DR PDBsum; 6W66; -.
DR PDBsum; 6WCQ; -.
DR PDBsum; 6WNX; -.
DR PDBsum; 7B5L; -.
DR PDBsum; 7B5M; -.
DR PDBsum; 7B5R; -.
DR PDBsum; 7T1Y; -.
DR PDBsum; 7T1Z; -.
DR AlphaFoldDB; P63208; -.
DR SMR; P63208; -.
DR BioGRID; 112391; 420.
DR CORUM; P63208; -.
DR DIP; DIP-31606N; -.
DR IntAct; P63208; 213.
DR MINT; P63208; -.
DR STRING; 9606.ENSP00000231487; -.
DR DrugBank; DB06980; (2S)-2-(1H-indol-3-yl)hexanoic acid.
DR DrugBank; DB06981; (2S)-2-(1H-indol-3-yl)pentanoic acid.
DR DrugBank; DB06982; (2S)-8-[(tert-butoxycarbonyl)amino]-2-(1H-indol-3-yl)octanoic acid.
DR DrugBank; DB01750; 1-naphthaleneacetic acid.
DR DrugBank; DB07950; Indoleacetic acid.
DR MoonDB; P63208; Predicted.
DR GlyGen; P63208; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P63208; -.
DR MetOSite; P63208; -.
DR PhosphoSitePlus; P63208; -.
DR SwissPalm; P63208; -.
DR BioMuta; SKP1; -.
DR DMDM; 52783797; -.
DR SWISS-2DPAGE; P63208; -.
DR EPD; P63208; -.
DR jPOST; P63208; -.
DR MassIVE; P63208; -.
DR MaxQB; P63208; -.
DR PaxDb; P63208; -.
DR PeptideAtlas; P63208; -.
DR PRIDE; P63208; -.
DR ProteomicsDB; 57504; -.
DR ProteomicsDB; 57505; -. [P63208-2]
DR TopDownProteomics; P63208-1; -. [P63208-1]
DR Antibodypedia; 4566; 563 antibodies from 39 providers.
DR DNASU; 6500; -.
DR Ensembl; ENST00000353411.11; ENSP00000231487.9; ENSG00000113558.19. [P63208-1]
DR Ensembl; ENST00000517625.5; ENSP00000429961.1; ENSG00000113558.19. [P63208-1]
DR Ensembl; ENST00000522552.5; ENSP00000429472.1; ENSG00000113558.19. [P63208-2]
DR Ensembl; ENST00000522855.5; ENSP00000429686.1; ENSG00000113558.19. [P63208-1]
DR GeneID; 6500; -.
DR KEGG; hsa:6500; -.
DR MANE-Select; ENST00000353411.11; ENSP00000231487.9; NM_170679.3; NP_733779.1.
DR UCSC; uc003kzc.5; human.
DR CTD; 6500; -.
DR DisGeNET; 6500; -.
DR GeneCards; SKP1; -.
DR HGNC; HGNC:10899; SKP1.
DR HPA; ENSG00000113558; Low tissue specificity.
DR MIM; 601434; gene.
DR neXtProt; NX_P63208; -.
DR OpenTargets; ENSG00000113558; -.
DR PharmGKB; PA162403424; -.
DR VEuPathDB; HostDB:ENSG00000113558; -.
DR eggNOG; KOG1724; Eukaryota.
DR GeneTree; ENSGT00390000012652; -.
DR InParanoid; P63208; -.
DR OMA; PLKSADM; -.
DR OrthoDB; 1412723at2759; -.
DR PhylomeDB; P63208; -.
DR TreeFam; TF354233; -.
DR BioCyc; MetaCyc:ENSG00000113558-MON; -.
DR PathwayCommons; P63208; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1170546; Prolactin receptor signaling.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2644607; Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P63208; -.
DR SIGNOR; P63208; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 6500; 659 hits in 1056 CRISPR screens.
DR ChiTaRS; SKP1; human.
DR EvolutionaryTrace; P63208; -.
DR GeneWiki; SKP1A; -.
DR GenomeRNAi; 6500; -.
DR Pharos; P63208; Tbio.
DR PRO; PR:P63208; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P63208; protein.
DR Bgee; ENSG00000113558; Expressed in prefrontal cortex and 209 other tissues.
DR ExpressionAtlas; P63208; baseline and differential.
DR Genevisible; P63208; HS.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097602; F:cullin family protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:1990444; F:F-box domain binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IPI:ParkinsonsUK-UCL.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR016897; SKP1.
DR InterPro; IPR001232; SKP1-like.
DR InterPro; IPR036296; SKP1-like_dim_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR016072; Skp1_comp_dimer.
DR InterPro; IPR016073; Skp1_comp_POZ.
DR PANTHER; PTHR11165; PTHR11165; 1.
DR Pfam; PF01466; Skp1; 1.
DR Pfam; PF03931; Skp1_POZ; 1.
DR PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
DR SMART; SM00512; Skp1; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF81382; SSF81382; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Host-virus interaction; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 2..163
FT /note="S-phase kinase-associated protein 1"
FT /id="PRO_0000187251"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..163
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 154..163
FT /note="RKENQWCEEK -> GSTQFCL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007555"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1FS1"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6M90"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1FS1"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:1FS1"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:1FS1"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6O60"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1FS1"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1LDK"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:1FS1"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5XYL"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6WNX"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:1FS1"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:1FS1"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:1FS1"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1FQV"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:1FS1"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:6M90"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2AST"
SQ SEQUENCE 163 AA; 18658 MW; C794D62AFB75528A CRC64;
MPSIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ
WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKVDQGTL FELILAANYL DIKGLLDVTC
KTVANMIKGK TPEEIRKTFN IKNDFTEEEE AQVRKENQWC EEK
