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SKR1_CAEEL
ID   SKR1_CAEEL              Reviewed;         176 AA.
AC   G5ECU1; Q8WSZ9;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Skp1-related protein {ECO:0000312|WormBase:F46A9.5};
GN   Name=skr-1 {ECO:0000312|WormBase:F46A9.5};
GN   ORFNames=F46A9.5 {ECO:0000312|WormBase:F46A9.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000312|EMBL:AAL34093.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-176, FUNCTION, INTERACTION WITH CUL-1, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11864567; DOI=10.1016/s0960-9822(02)00682-6;
RA   Nayak S., Santiago F.E., Jin H., Lin D., Schedl T., Kipreos E.T.;
RT   "The Caenorhabditis elegans Skp1-related gene family: diverse functions in
RT   cell proliferation, morphogenesis, and meiosis.";
RL   Curr. Biol. 12:277-287(2002).
RN   [3] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH CUL-1 AND MEC-15, TISSUE SPECIFICITY, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11864566; DOI=10.1016/s0960-9822(02)00657-7;
RA   Yamanaka A., Yada M., Imaki H., Koga M., Ohshima Y., Nakayama K.;
RT   "Multiple Skp1-related proteins in Caenorhabditis elegans: diverse patterns
RT   of interaction with Cullins and F-box proteins.";
RL   Curr. Biol. 12:267-275(2002).
RN   [4] {ECO:0000305}
RP   INTERACTION WITH DRE-1.
RX   PubMed=17336909; DOI=10.1016/j.devcel.2007.01.018;
RA   Fielenbach N., Guardavaccaro D., Neubert K., Chan T., Li D., Feng Q.,
RA   Hutter H., Pagano M., Antebi A.;
RT   "DRE-1: an evolutionarily conserved F box protein that regulates C. elegans
RT   developmental age.";
RL   Dev. Cell 12:443-455(2007).
RN   [5] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH SYG-1, AND DISRUPTION PHENOTYPE.
RX   PubMed=17626846; DOI=10.1126/science.1145727;
RA   Ding M., Chao D., Wang G., Shen K.;
RT   "Spatial regulation of an E3 ubiquitin ligase directs selective synapse
RT   elimination.";
RL   Science 317:947-951(2007).
RN   [6] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18340346; DOI=10.1038/cdd.2008.30;
RA   Gao M.X., Liao E.H., Yu B., Wang Y., Zhen M., Derry W.B.;
RT   "The SCF FSN-1 ubiquitin ligase controls germline apoptosis through CEP-
RT   1/p53 in C. elegans.";
RL   Cell Death Differ. 15:1054-1062(2008).
RN   [7] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH SEL-10, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   MET-140.
RX   PubMed=18718460; DOI=10.1016/j.ydbio.2008.07.035;
RA   Killian D.J., Harvey E., Johnson P., Otori M., Mitani S., Xue D.;
RT   "SKR-1, a homolog of Skp1 and a member of the SCF(SEL-10) complex,
RT   regulates sex-determination and LIN-12/Notch signaling in C. elegans.";
RL   Dev. Biol. 322:322-331(2008).
CC   -!- FUNCTION: Probable essential component of SCF (SKP1-CUL1-F-box protein)
CC       E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination
CC       and subsequent proteasomal degradation of target proteins
CC       (PubMed:17626846). Regulates cell proliferation during embryonic and
CC       larval development (PubMed:11864567, PubMed:11864566). Involved in
CC       synapse elimination in early synapse development (PubMed:17626846). May
CC       negatively regulate the apoptotic activity of cep-1 in response to
CC       genotoxic stress (PubMed:18340346). Plays a role in sex determination
CC       (PubMed:18718460). {ECO:0000269|PubMed:11864566,
CC       ECO:0000269|PubMed:11864567, ECO:0000269|PubMed:17626846,
CC       ECO:0000269|PubMed:18340346, ECO:0000269|PubMed:18718460}.
CC   -!- SUBUNIT: Probable component of the SCF(sel-10) E3 ubiquitin-protein
CC       ligase complex containing F-box domain-containing protein sel-10 as the
CC       substrate recognition component (PubMed:17626846). Interacts with cul-1
CC       (PubMed:11864567, PubMed:11864566). May interact with the F-box protein
CC       mec-15 (PubMed:11864566). Interacts with dre-1 (PubMed:17336909).
CC       Interacts with syg-1 (PubMed:17626846). Interacts with sel-10
CC       (PubMed:18718460). {ECO:0000250|UniProtKB:P63208,
CC       ECO:0000269|PubMed:11864566, ECO:0000269|PubMed:11864567,
CC       ECO:0000269|PubMed:17336909, ECO:0000269|PubMed:17626846,
CC       ECO:0000269|PubMed:18718460}.
CC   -!- INTERACTION:
CC       G5ECU1; Q17962: CELE_C14B1.3; NbExp=3; IntAct=EBI-323117, EBI-2003707;
CC       G5ECU1; Q94251: dre-1; NbExp=3; IntAct=EBI-323117, EBI-314286;
CC       G5ECU1; G5EDX9: fbxa-101; NbExp=4; IntAct=EBI-323117, EBI-2003730;
CC       G5ECU1; O17198: fbxa-164; NbExp=4; IntAct=EBI-323117, EBI-2412975;
CC       G5ECU1; O16525: fbxa-196; NbExp=5; IntAct=EBI-323117, EBI-329491;
CC       G5ECU1; Q2YS43: fog-2; NbExp=4; IntAct=EBI-323117, EBI-2417735;
CC       G5ECU1; Q18223: fsn-1; NbExp=4; IntAct=EBI-323117, EBI-2003744;
CC       G5ECU1; Q93794: sel-10; NbExp=5; IntAct=EBI-323117, EBI-323098;
CC       G5ECU1; P91305: xrep-4; NbExp=3; IntAct=EBI-323117, EBI-2003766;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in the adult.
CC       {ECO:0000269|PubMed:11864566}.
CC   -!- DISRUPTION PHENOTYPE: The majority of animals are either embryonic or
CC       larval lethal. Rare surviving animals develop into uncoordinated
CC       sterile adults with hyperplasia of tissues including the uterus and the
CC       spermatheca of the somatic gonad (PubMed:18718460). RNAi-mediated
CC       knockdown results in a reduction in brood size of the injected parent
CC       and embryonic lethality of offspring between gastrulation and the two-
CC       cell phase of embryogenesis (PubMed:11864566). RNAi-mediated knockdown
CC       causes synapse clusters that are retained rather than eliminated in the
CC       secondary synapse region, anterior to the vulva during synapse
CC       development (PubMed:17626846). RNAi-mediated knockdown leads to an
CC       increase in germ cell apoptosis in response to genotoxic stress
CC       (PubMed:18340346). RNAi-mediated knockdown within 16 hours of RNAi
CC       administration results in defects in embryonic divisions including
CC       spindle mispositioning, abnormal polar bodies and ectopic furrows, and
CC       hyperplasia of the somatic gonad and hypodermis in larvae
CC       (PubMed:11864567). All embryos laid 16 hours post RNAi treatment arrest
CC       and contain almost twice the number of cells as wild-type embryos
CC       (PubMed:11864567). Zygotic RNAi-mediated knockdown results in 90%
CC       sterility (PubMed:11864567). {ECO:0000269|PubMed:11864566,
CC       ECO:0000269|PubMed:11864567, ECO:0000269|PubMed:17626846,
CC       ECO:0000269|PubMed:18340346, ECO:0000269|PubMed:18718460}.
CC   -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000305}.
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DR   EMBL; BX284601; CAB03110.1; -; Genomic_DNA.
DR   EMBL; AF440505; AAL34093.1; -; mRNA.
DR   PIR; T21573; T21573.
DR   RefSeq; NP_492513.1; NM_060112.5.
DR   AlphaFoldDB; G5ECU1; -.
DR   SMR; G5ECU1; -.
DR   ComplexPortal; CPX-958; SCF-rpm-1 ubiquitin ligase complex.
DR   IntAct; G5ECU1; 20.
DR   MINT; G5ECU1; -.
DR   STRING; 6239.F46A9.5.3; -.
DR   EPD; G5ECU1; -.
DR   PaxDb; G5ECU1; -.
DR   PeptideAtlas; G5ECU1; -.
DR   EnsemblMetazoa; F46A9.5.1; F46A9.5.1; WBGene00004807.
DR   GeneID; 172775; -.
DR   KEGG; cel:CELE_F46A9.5; -.
DR   UCSC; F46A9.5.1; c. elegans.
DR   CTD; 172775; -.
DR   WormBase; F46A9.5; CE10580; WBGene00004807; skr-1.
DR   eggNOG; KOG1724; Eukaryota.
DR   GeneTree; ENSGT00390000012652; -.
DR   HOGENOM; CLU_059252_4_0_1; -.
DR   InParanoid; G5ECU1; -.
DR   OMA; PLKSADM; -.
DR   OrthoDB; 1412723at2759; -.
DR   PhylomeDB; G5ECU1; -.
DR   Reactome; R-CEL-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR   Reactome; R-CEL-69231; Cyclin D associated events in G1.
DR   Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-CEL-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-CEL-8951664; Neddylation.
DR   Reactome; R-CEL-917937; Iron uptake and transport.
DR   Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; G5ECU1; -.
DR   PRO; PR:G5ECU1; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00004807; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:ComplexPortal.
DR   GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR   GO; GO:0046660; P:female sex differentiation; IGI:UniProtKB.
DR   GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:UniProtKB.
DR   GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IGI:WormBase.
DR   GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:WormBase.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR   GO; GO:0090128; P:regulation of synapse maturation; IC:ComplexPortal.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
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   Developmental protein; Neurogenesis; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..176
FT                   /note="Skp1-related protein"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000433874"
FT   MUTAGEN         140
FT                   /note="M->I: In sm151; weak loss of function mutation, does
FT                   not bind to sel-10 protein."
FT                   /evidence="ECO:0000269|PubMed:18718460"
SQ   SEQUENCE   176 AA;  20032 MW;  3FCDC4D52BC2DF35 CRC64;
     MADQKKVSEA AKEREIKISS SDNEIFLVPR NVIRLSNTIN TLLMDLGLDD EEGTNAEPIP
     VQNVTASILK KVISWCNHHH SDPISTEDSD NREKRTDDIG SWDVEFLKVD QGTLFELILA
     ANYLDIKGLL DVTCKTVANM IKGKSPEEIR RTFNIKNDFT PEEEEQIRKE NAWCED
 
 
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