ID   E7ERH2_HUMAN            Unreviewed;       142 AA.
AC   E7ERH2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=S-phase kinase-associated protein 1 {ECO:0000256|ARBA:ARBA00014544};
DE   AltName: Full=Cyclin-A/CDK2-associated protein p19 {ECO:0000256|ARBA:ARBA00033452};
DE   AltName: Full=p19skp1 {ECO:0000256|ARBA:ARBA00033118};
DE   Flags: Fragment;
GN   Name=SKP1 {ECO:0000313|Ensembl:ENSP00000429415.1};
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:ENSP00000429415.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000429415.1, 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: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   [7] {ECO:0000313|Ensembl:ENSP00000429415.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the SKP1 family.
CC       {ECO:0000256|ARBA:ARBA00009993}.
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DR   EMBL; AC011336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E7ERH2; -.
DR   SMR; E7ERH2; -.
DR   IntAct; E7ERH2; 1.
DR   MassIVE; E7ERH2; -.
DR   MaxQB; E7ERH2; -.
DR   PeptideAtlas; E7ERH2; -.
DR   ProteomicsDB; 17779; -.
DR   Antibodypedia; 4566; 602 antibodies from 39 providers.
DR   Ensembl; ENST00000519321.5; ENSP00000429415.1; ENSG00000113558.19.
DR   UCSC; uc063hai.1; human.
DR   HGNC; HGNC:10899; SKP1.
DR   VEuPathDB; HostDB:ENSG00000113558; -.
DR   GeneTree; ENSGT00390000012652; -.
DR   HOGENOM; CLU_059252_7_0_1; -.
DR   OMA; MREIEKP; -.
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; E7ERH2; baseline and differential.
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|PIRSR:PIRSR028729-50};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:E7ERH2,
KW   ECO:0007829|ProteomicsDB:E7ERH2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Ubl conjugation {ECO:0000256|PIRSR:PIRSR028729-50};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          2..67
FT                   /note="SKP1 component POZ"
FT                   /evidence="ECO:0000259|Pfam:PF03931"
FT   DOMAIN          113..142
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"
FT   NON_TER         142
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000429415.1"
SQ   SEQUENCE   142 AA;  16034 MW;  229D2563CA67C179 CRC64;
     MPSIKLQSSD GEIFEVDVEI AKQSVTIKTM LEDLGMDDEG DDDPVPLPNV NAAILKKVIQ
     WCTHHKDDPP PPEDDENKEK RTDDIPVWDQ EFLKVDQGTL FELILAANYL DIKGLLDVTC
     KTVANMIKGK TPEEIRKTFN IK
//