ID   E5RI56_HUMAN            Unreviewed;       197 AA.
AC   E5RI56;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 2.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=S-phase kinase-associated protein 1 {ECO:0000256|PIRNR:PIRNR028729};
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:ENSP00000430774.2, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000430774.2, 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:0000313|Ensembl:ENSP00000430774.2}
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}.
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DR   EMBL; AC011336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E5RI56; -.
DR   SMR; E5RI56; -.
DR   STRING; 9606.ENSP00000430774; -.
DR   BioMuta; ENSG00000272772; -.
DR   MassIVE; E5RI56; -.
DR   PaxDb; 9606-ENSP00000430774; -.
DR   PeptideAtlas; E5RI56; -.
DR   ProteomicsDB; 16191; -.
DR   Ensembl; ENST00000519718.2; ENSP00000430774.2; ENSG00000272772.2.
DR   UCSC; uc063hak.1; human.
DR   GeneCards; ENSG00000272772; -.
DR   VEuPathDB; HostDB:ENSG00000272772; -.
DR   eggNOG; KOG0371; Eukaryota.
DR   eggNOG; KOG1724; Eukaryota.
DR   HOGENOM; CLU_2432580_0_0_1; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; E5RI56; Protein.
DR   Bgee; ENSG00000272772; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 86 other cell types or tissues.
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   3: Inferred from homology;
KW   Isopeptide bond {ECO:0000256|PIRNR:PIRNR028729,
KW   ECO:0000256|PIRSR:PIRSR028729-50};
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          36..101
FT                   /note="SKP1 component POZ"
FT                   /evidence="ECO:0000259|Pfam:PF03931"
FT   DOMAIN          147..194
FT                   /note="SKP1 component dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF01466"
FT   CROSSLNK        176
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028729-50"
SQ   SEQUENCE   197 AA;  22728 MW;  5C720F6A71BBC85D CRC64;
     MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKMPSIKL QSSDGEIFEV DVEIAKQSVT
     IKTMLEDLGM DDEGDDDPVP LPNVNAAILK KVIQWCTHHK DDPPPPEDDE NKEKRTDDIP
     VWDQEFLKVD QGTLFELILA ANYLDIKGLL DVTCKTVANM IKGKTPEEIR KTFNIKNDFT
     EEEEAQVRKE NQWCEEK
//