SKP1_MOUSE
ID SKP1_MOUSE Reviewed; 163 AA.
AC Q9WTX5; Q8C5H6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=S-phase kinase-associated protein 1;
DE AltName: Full=Cyclin-A/CDK2-associated protein p19;
DE AltName: Full=S-phase kinase-associated protein 1A;
DE AltName: Full=p19A;
DE AltName: Full=p19skp1;
GN Name=Skp1 {ECO:0000303|PubMed:10097128, ECO:0000312|MGI:MGI:103575};
GN Synonyms=Skp1a {ECO:0000312|MGI:MGI:103575};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH
RP CUL1; PHOSPHORYLATED NFKBIA AND BTRC.
RC STRAIN=C57BL/6J;
RX PubMed=10097128; DOI=10.1073/pnas.96.7.3859;
RA Hatakeyama S., Kitagawa M., Nakayama K., Shirane M., Matsumoto M.,
RA Hattori K., Higashi H., Nakano H., Okumura K., Onoe K., Good R.A.,
RA Nakayama K.;
RT "Ubiquitin-dependent degradation of IkappaBalpha is mediated by a ubiquitin
RT ligase Skp1/Cul 1/F-box protein FWD1.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3859-3863(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Brain, Head, Kidney, Olfactory bulb, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH PHOSPHORYLATED NFKBIA; BTRC
RP AND RELA.
RX PubMed=9990853; DOI=10.1101/gad.13.3.284;
RA Spencer E., Jiang J., Chen Z.J.;
RT "Signal-induced ubiquitination of IkappaBalpha by the F-box protein
RT Slimb/beta-TrCP.";
RL Genes Dev. 13:284-294(1999).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH BTRC AND CUL1.
RX PubMed=11735228; DOI=10.1006/geno.2001.6658;
RA Maruyama S., Hatakeyama S., Nakayama K., Ishida N., Kawakami K.,
RA Nakayama K.;
RT "Characterization of a mouse gene (Fbxw6) that encodes a homologue of
RT Caenorhabditis elegans SEL-10.";
RL Genomics 78:214-222(2001).
RN [6]
RP FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12140560; DOI=10.1038/nature00890;
RA Yoshida Y., Chiba T., Tokunaga F., Kawasaki H., Iwai K., Suzuki T., Ito Y.,
RA Matsuoka K., Yoshida M., Tanaka K., Tai T.;
RT "E3 ubiquitin ligase that recognizes sugar chains.";
RL Nature 418:438-442(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH FBXO45.
RX PubMed=19996097; DOI=10.1074/jbc.m109.046284;
RA Tada H., Okano H.J., Takagi H., Shibata S., Yao I., Matsumoto M., Saiga T.,
RA Nakayama K.I., Kashima H., Takahashi T., Setou M., Okano H.;
RT "Fbxo45, a novel ubiquitin ligase, regulates synaptic activity.";
RL J. Biol. Chem. 285:3840-3849(2010).
RN [9]
RP IDENTIFICATION IN AN SCF COMPLEX, AND INTERACTION WITH FBXW15.
RX PubMed=23319590; DOI=10.1074/jbc.m112.426882;
RA Zou C., Chen Y., Smith R.M., Snavely C., Li J., Coon T.A., Chen B.B.,
RA Zhao Y., Mallampalli R.K.;
RT "SCF(Fbxw15) mediates histone acetyltransferase binding to origin
RT recognition complex (HBO1) ubiquitin-proteasomal degradation to regulate
RT cell proliferation.";
RL J. Biol. Chem. 288:6306-6316(2013).
RN [10]
RP DEGRADATION VIA AUTOPHAGY.
RX PubMed=29937374; DOI=10.1016/j.cmet.2018.05.023;
RA Toledo M., Batista-Gonzalez A., Merheb E., Aoun M.L., Tarabra E., Feng D.,
RA Sarparanta J., Merlo P., Botre F., Schwartz G.J., Pessin J.E., Singh R.;
RT "Autophagy regulates the liver clock and glucose metabolism by degrading
RT CRY1.";
RL Cell Metab. 28:268-281(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 SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is
CC involved in regulation of G1/S transition. SCF(SKP2) directs
CC ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and
CC probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E,
CC NOTCH1 released notch intracellular domain (NICD), and probably PSEN1.
CC SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs
CC ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and
CC DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs
CC ubiquitination of BCL6 and DTL but does not seem to direct
CC ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA
CC at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-
CC RELA dimer to translocate into the nucleus and to activate
CC transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3)
CC and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9)
CC directs ubiquitination of TTI1 and TELO2 (By similarity).
CC {ECO:0000250|UniProtKB:P63208, ECO:0000269|PubMed:10097128,
CC ECO:0000269|PubMed:12140560, ECO:0000269|PubMed:9990853}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with KDM2B, forming heterodimers (By similarity).
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) (By similarity). 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. Component of the
CC SCF(FBXW15) complex containing FBXW15 (PubMed:23319590). Interacts with
CC CEP68 (By similarity). Interacts with FBXW15 (PubMed:23319590).
CC Interacts with NOTCH2 (By similarity). The SKP1-KDM2A and SKP1-KDM2B
CC complexes interact with UBB (By similarity).
CC {ECO:0000250|UniProtKB:P63208, ECO:0000269|PubMed:10097128,
CC ECO:0000269|PubMed:11735228, ECO:0000269|PubMed:12140560,
CC ECO:0000269|PubMed:19996097, ECO:0000269|PubMed:23319590,
CC ECO:0000269|PubMed:9990853}.
CC -!- INTERACTION:
CC Q9WTX5; Q9QXW2: Fbxw5; NbExp=2; IntAct=EBI-1202363, EBI-16031930;
CC Q9WTX5; P62137: Ppp1ca; NbExp=2; IntAct=EBI-1202363, EBI-357187;
CC Q9WTX5; Q9CQJ4: Rnf2; NbExp=4; IntAct=EBI-1202363, EBI-927321;
CC Q9WTX5; Q9UKT7: FBXL3; Xeno; NbExp=4; IntAct=EBI-1202363, EBI-2557269;
CC -!- PTM: Undergoes autophagy-mediated degradation in the liver in a time-
CC dependent manner. {ECO:0000269|PubMed:29937374}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR EMBL; AF083214; AAD16036.1; -; mRNA.
DR EMBL; AK002983; BAB22496.1; -; mRNA.
DR EMBL; AK010628; BAB27074.1; -; mRNA.
DR EMBL; AK012498; BAB28281.1; -; mRNA.
DR EMBL; AK014245; BAB29222.1; -; mRNA.
DR EMBL; AK027909; BAC25660.1; -; mRNA.
DR EMBL; AK078330; BAC37220.1; -; mRNA.
DR EMBL; AK088339; BAC40292.1; -; mRNA.
DR EMBL; BC002115; AAH02115.1; -; mRNA.
DR CCDS; CCDS24669.1; -.
DR RefSeq; NP_035673.3; NM_011543.4.
DR RefSeq; XP_006532849.1; XM_006532786.2.
DR AlphaFoldDB; Q9WTX5; -.
DR SMR; Q9WTX5; -.
DR BioGRID; 203998; 106.
DR CORUM; Q9WTX5; -.
DR DIP; DIP-38596N; -.
DR IntAct; Q9WTX5; 54.
DR MINT; Q9WTX5; -.
DR STRING; 10090.ENSMUSP00000038744; -.
DR iPTMnet; Q9WTX5; -.
DR PhosphoSitePlus; Q9WTX5; -.
DR SwissPalm; Q9WTX5; -.
DR REPRODUCTION-2DPAGE; Q9WTX5; -.
DR EPD; Q9WTX5; -.
DR jPOST; Q9WTX5; -.
DR MaxQB; Q9WTX5; -.
DR PaxDb; Q9WTX5; -.
DR PRIDE; Q9WTX5; -.
DR ProteomicsDB; 261188; -.
DR Antibodypedia; 4566; 563 antibodies from 39 providers.
DR DNASU; 21402; -.
DR Ensembl; ENSMUST00000037324; ENSMUSP00000038744; ENSMUSG00000036309.
DR Ensembl; ENSMUST00000109072; ENSMUSP00000104700; ENSMUSG00000036309.
DR GeneID; 21402; -.
DR KEGG; mmu:21402; -.
DR UCSC; uc007ivf.2; mouse.
DR CTD; 6500; -.
DR MGI; MGI:103575; Skp1.
DR VEuPathDB; HostDB:ENSMUSG00000036309; -.
DR eggNOG; KOG1724; Eukaryota.
DR GeneTree; ENSGT00390000012652; -.
DR InParanoid; Q9WTX5; -.
DR OMA; PLKSADM; -.
DR OrthoDB; 1412723at2759; -.
DR PhylomeDB; Q9WTX5; -.
DR TreeFam; TF354233; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1170546; Prolactin receptor signaling.
DR Reactome; R-MMU-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR Reactome; R-MMU-9708530; Regulation of BACH1 activity.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 21402; 23 hits in 71 CRISPR screens.
DR ChiTaRS; Skp1a; mouse.
DR PRO; PR:Q9WTX5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WTX5; protein.
DR Bgee; ENSMUSG00000036309; Expressed in vestibular membrane of cochlear duct and 261 other tissues.
DR ExpressionAtlas; Q9WTX5; baseline and differential.
DR Genevisible; Q9WTX5; MM.
DR GO; GO:0005813; C:centrosome; IDA:CACAO.
DR GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031519; C:PcG protein complex; ISO:MGI.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0097602; F:cullin family protein binding; ISO:MGI.
DR GO; GO:1990444; F:F-box domain binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IC:MGI.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISO:MGI.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:MGI.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:MGI.
DR GO; GO:0006513; P:protein monoubiquitination; IGI:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:MGI.
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 Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..163
FT /note="S-phase kinase-associated protein 1"
FT /id="PRO_0000187252"
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:21183079"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P63208"
FT CONFLICT 41
FT /note="D -> N (in Ref. 2; BAC37220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 163 AA; 18672 MW; AE184C00BE6556DB CRC64;
MPTIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ
WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKVDQGTL FELILAANYL DIKGLLDVTC
KTVANMIKGK TPEEIRKTFN IKNDFTEEEE AQVRKENQWC EEK
