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KLH22_XENTR
ID   KLH22_XENTR             Reviewed;         641 AA.
AC   Q08CY1;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Kelch-like protein 22 {ECO:0000305};
GN   Name=klhl22;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Oviduct;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC       ubiquitin ligase complex. The BCR(KLHL22) ubiquitin ligase complex
CC       could mediate the monoubiquitination of PLK1 and regulate its activity
CC       in spindle assembly checkpoint (SAC) and chromosome segregation. The
CC       BCR(KLHL22) ubiquitin ligase complex may also be responsible for the
CC       ubiquitin-dependent proteasomal degradation of DEPDC5 and the
CC       activation of the TORC1 pathway. {ECO:0000250|UniProtKB:Q53GT1}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q53GT1}.
CC   -!- SUBUNIT: Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at
CC       least composed of cul3, klhl22 and rbx1.
CC       {ECO:0000250|UniProtKB:Q53GT1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q53GT1}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q53GT1}.
CC       Nucleus {ECO:0000250|UniProtKB:Q53GT1}. Lysosome
CC       {ECO:0000250|UniProtKB:Q53GT1}.
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DR   EMBL; BC124036; AAI24037.1; -; mRNA.
DR   RefSeq; NP_001072910.1; NM_001079442.1.
DR   RefSeq; XP_012821760.1; XM_012966306.2.
DR   RefSeq; XP_012821764.1; XM_012966310.2.
DR   AlphaFoldDB; Q08CY1; -.
DR   SMR; Q08CY1; -.
DR   STRING; 8364.ENSXETP00000009275; -.
DR   PaxDb; Q08CY1; -.
DR   DNASU; 780372; -.
DR   GeneID; 780372; -.
DR   KEGG; xtr:780372; -.
DR   CTD; 84861; -.
DR   Xenbase; XB-GENE-948974; klhl22.
DR   eggNOG; KOG4441; Eukaryota.
DR   HOGENOM; CLU_004253_14_3_1; -.
DR   InParanoid; Q08CY1; -.
DR   OrthoDB; 250404at2759; -.
DR   Reactome; R-XTR-8951664; Neddylation.
DR   Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005827; C:polar microtubule; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR   Gene3D; 2.120.10.80; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR017096; BTB-kelch_protein.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR030575; KLHL22.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR45632:SF5; PTHR45632:SF5; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 3.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 6.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kelch repeat; Lysosome;
KW   Mitosis; Nucleus; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..641
FT                   /note="Kelch-like protein 22"
FT                   /id="PRO_0000396636"
FT   DOMAIN          50..117
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REPEAT          299..349
FT                   /note="Kelch 1"
FT   REPEAT          350..399
FT                   /note="Kelch 2"
FT   REPEAT          400..446
FT                   /note="Kelch 3"
FT   REPEAT          448..493
FT                   /note="Kelch 4"
FT   REPEAT          494..544
FT                   /note="Kelch 5"
FT   REPEAT          545..593
FT                   /note="Kelch 6"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   641 AA;  72725 MW;  3C544A1DED2CA506 CRC64;
     MAEDLETMKP SQAPQQPSLP QGSSKTYRSA EHSQALLSGL VALRDSGILF DVVLKVEGKS
     IEAHRILLAA SCDYFRGMFA GGLKEMDQRE VQIHGVSYSA MCRIMDFIYT SDLALSVNNV
     QETLTAACQL QISEVIQFCC DFLVSWVDEE NVLELYKLAD IFHLNRLTEQ LDTFVLKNFI
     TFSQTQMYRQ LPLDKVFSLL NSNRLEVASE NEVYEGALLY HYTPEQLEKD QVSLLESPKL
     LEAVRFPLMD LAILQRLHDK LGLCPLKTTV LKALEYHKNE SMQPVMQGPN TQLRSEFHCV
     VGFGGMYSAP YTVLSDQVKY LNPLLGEWRP LTAPHAPRMS NQGIAVLNNF VYLIGGDNNV
     RGYRAEARCW RYDPRHSRWF QIQSMQQPRA DLSVCVLGDF LYAVAGRDYH DELKEVERYD
     PFTNTWEYVA PLQKQVHAHA AAALDGRMYV ACGRRGNTYL KDTFCYDPER DQWASVALSP
     VRRAWHGMAA LQEKIYLIGG SNDDEGFRQD VLEVACYSPK TDQWTLVSPL PAGHGEPGIA
     VLAKKIFVLG GRSHNQGDRT DYVHVYEAER DYWEDGPRLE DDISGMAACV LTLPRSVLMD
     TDVWTQEMYM QYMDPVQNLA DNASEVMSVS DWEDLDNSGE D
 
 
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