ID E5RJR5_HUMAN Unreviewed; 163 AA. AC E5RJR5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=S-phase kinase-associated protein 1 {ECO:0000256|PIRNR:PIRNR028729}; GN Name=SKP1 {ECO:0000313|Ensembl:ENSP00000431067.1}; 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 {ECO:0000313|Ensembl:ENSP00000431067.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000431067.1, ECO:0000313|Proteomes:UP000005640} 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 [2] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [3] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [4] {ECO:0007829|PubMed:21406692} RP IDENTIFICATION BY 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 [5] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [6] {ECO:0007829|PubMed:25114211} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; 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 [7] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; 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 [8] {ECO:0000313|Ensembl:ENSP00000431067.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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. {ECO:0000256|PIRNR:PIRNR028729}. CC -!- FUNCTION: The functional specificity of the SCF complex depends on the CC F-box protein as substrate recognition component. CC {ECO:0000256|PIRNR:PIRNR028729}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|PIRNR:PIRNR028729}. CC -!- SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin- CC protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F- CC box domain-containing protein as substrate-specific subunit. CC {ECO:0000256|PIRNR:PIRNR028729}. CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000256|ARBA:ARBA00009993, CC ECO:0000256|PIRNR:PIRNR028729}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC011336; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104109; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; E5RJR5; -. DR SMR; E5RJR5; -. DR MassIVE; E5RJR5; -. DR MaxQB; E5RJR5; -. DR PeptideAtlas; E5RJR5; -. DR ProteomicsDB; 16686; -. DR Antibodypedia; 4566; 602 antibodies from 39 providers. DR Ensembl; ENST00000521216.5; ENSP00000431067.1; ENSG00000113558.19. DR UCSC; uc063hab.1; human. DR HGNC; HGNC:10899; SKP1. DR VEuPathDB; HostDB:ENSG00000113558; -. DR GeneTree; ENSGT00390000012652; -. DR PhylomeDB; E5RJR5; -. DR UniPathway; UPA00143; -. DR ChiTaRS; SKP1; human. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000113558; Expressed in prefrontal cortex and 211 other cell types or tissues. DR ExpressionAtlas; E5RJR5; baseline and differential. DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:UniProtKB-UniRule. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR CDD; cd18322; BTB_POZ_SKP1; 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:SF24; S-PHASE KINASE-ASSOCIATED PROTEIN 1; 1. DR PANTHER; PTHR11165; SKP1; 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; POZ domain; 1. DR SUPFAM; SSF81382; Skp1 dimerisation domain-like; 1. PE 1: Evidence at protein level; KW Isopeptide bond {ECO:0000256|PIRNR:PIRNR028729, KW ECO:0000256|PIRSR:PIRSR028729-50}; KW Proteomics identification {ECO:0007829|PeptideAtlas:E5RJR5, KW ECO:0007829|ProteomicsDB:E5RJR5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Ubl conjugation {ECO:0000256|PIRNR:PIRNR028729, KW ECO:0000256|PIRSR:PIRSR028729-50}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|PIRNR:PIRNR028729}. FT DOMAIN 2..67 FT /note="SKP1 component POZ" FT /evidence="ECO:0000259|Pfam:PF03931" FT DOMAIN 113..160 FT /note="SKP1 component dimerisation" FT /evidence="ECO:0000259|Pfam:PF01466" FT REGION 63..83 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CROSSLNK 142 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000256|PIRSR:PIRSR028729-50" SQ SEQUENCE 163 AA; 18720 MW; 0738985C1D105178 CRC64; MPSIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKYTLRKT TVSLQAANYL DIKGLLDVTC KTVANMIKGK TPEEIRKTFN IKNDFTEEEE AQVRKENQWC EEK //