KLH11_HUMAN
ID KLH11_HUMAN Reviewed; 708 AA.
AC Q9NVR0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Kelch-like protein 11;
DE Flags: Precursor;
GN Name=KLHL11;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 67-340 IN COMPLEX WITH CUL3,
RP SUBUNIT, AND INTERACTION WITH CUL3.
RX PubMed=23349464; DOI=10.1074/jbc.m112.437996;
RA Canning P., Cooper C.D., Krojer T., Murray J.W., Pike A.C., Chaikuad A.,
RA Keates T., Thangaratnarajah C., Hojzan V., Marsden B.D., Gileadi O.,
RA Knapp S., von Delft F., Bullock A.N.;
RT "Structural basis for Cul3 assembly with the BTB-Kelch family of E3
RT ubiquitin ligases.";
RL J. Biol. Chem. 288:7803-7814(2013).
CC -!- FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex that mediates the ubiquitination of
CC target proteins, leading most often to their proteasomal degradation.
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex (By similarity). Homodimer. Interacts
CC with CUL3. {ECO:0000250, ECO:0000269|PubMed:23349464}.
CC -!- INTERACTION:
CC Q9NVR0; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-2691832, EBI-8638439;
CC Q9NVR0; P78424: POU6F2; NbExp=3; IntAct=EBI-2691832, EBI-12029004;
CC Q9NVR0; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2691832, EBI-947187;
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DR EMBL; AK001434; BAA91689.1; -; mRNA.
DR EMBL; BC034470; AAH34470.1; -; mRNA.
DR CCDS; CCDS11411.1; -.
DR RefSeq; NP_060613.1; NM_018143.2.
DR PDB; 3I3N; X-ray; 2.60 A; A/B=67-340.
DR PDB; 4AP2; X-ray; 2.80 A; A=67-340.
DR PDB; 4APF; X-ray; 3.10 A; A=67-340.
DR PDBsum; 3I3N; -.
DR PDBsum; 4AP2; -.
DR PDBsum; 4APF; -.
DR AlphaFoldDB; Q9NVR0; -.
DR SMR; Q9NVR0; -.
DR BioGRID; 120474; 70.
DR IntAct; Q9NVR0; 12.
DR STRING; 9606.ENSP00000314608; -.
DR iPTMnet; Q9NVR0; -.
DR PhosphoSitePlus; Q9NVR0; -.
DR BioMuta; KLHL11; -.
DR DMDM; 74734542; -.
DR EPD; Q9NVR0; -.
DR jPOST; Q9NVR0; -.
DR MassIVE; Q9NVR0; -.
DR MaxQB; Q9NVR0; -.
DR PaxDb; Q9NVR0; -.
DR PeptideAtlas; Q9NVR0; -.
DR PRIDE; Q9NVR0; -.
DR ProteomicsDB; 82847; -.
DR Antibodypedia; 16791; 105 antibodies from 23 providers.
DR DNASU; 55175; -.
DR Ensembl; ENST00000319121.4; ENSP00000314608.3; ENSG00000178502.6.
DR GeneID; 55175; -.
DR KEGG; hsa:55175; -.
DR MANE-Select; ENST00000319121.4; ENSP00000314608.3; NM_018143.3; NP_060613.1.
DR UCSC; uc002hyf.2; human.
DR CTD; 55175; -.
DR DisGeNET; 55175; -.
DR GeneCards; KLHL11; -.
DR HGNC; HGNC:19008; KLHL11.
DR HPA; ENSG00000178502; Low tissue specificity.
DR MIM; 619078; gene.
DR neXtProt; NX_Q9NVR0; -.
DR OpenTargets; ENSG00000178502; -.
DR PharmGKB; PA38777; -.
DR VEuPathDB; HostDB:ENSG00000178502; -.
DR eggNOG; KOG1072; Eukaryota.
DR GeneTree; ENSGT00940000159275; -.
DR HOGENOM; CLU_024322_0_0_1; -.
DR InParanoid; Q9NVR0; -.
DR OMA; AVIIRYD; -.
DR OrthoDB; 789713at2759; -.
DR PhylomeDB; Q9NVR0; -.
DR TreeFam; TF331981; -.
DR PathwayCommons; Q9NVR0; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9NVR0; -.
DR BioGRID-ORCS; 55175; 255 hits in 1109 CRISPR screens.
DR ChiTaRS; KLHL11; human.
DR EvolutionaryTrace; Q9NVR0; -.
DR GenomeRNAi; 55175; -.
DR Pharos; Q9NVR0; Tbio.
DR PRO; PR:Q9NVR0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9NVR0; protein.
DR Bgee; ENSG00000178502; Expressed in sperm and 104 other tissues.
DR ExpressionAtlas; Q9NVR0; baseline and differential.
DR Genevisible; Q9NVR0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 4.
DR SUPFAM; SSF117281; SSF117281; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Kelch repeat; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Ubl conjugation pathway.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..708
FT /note="Kelch-like protein 11"
FT /id="PRO_0000243918"
FT DOMAIN 94..170
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 205..307
FT /note="BACK"
FT REPEAT 360..407
FT /note="Kelch 1"
FT REPEAT 408..453
FT /note="Kelch 2"
FT REPEAT 455..501
FT /note="Kelch 3"
FT REPEAT 503..556
FT /note="Kelch 4"
FT REPEAT 610..661
FT /note="Kelch 5"
FT REGION 47..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:3I3N"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:3I3N"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:3I3N"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3I3N"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4AP2"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:4AP2"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:3I3N"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:3I3N"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:3I3N"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:3I3N"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:3I3N"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:3I3N"
FT HELIX 316..331
FT /evidence="ECO:0007829|PDB:3I3N"
SQ SEQUENCE 708 AA; 80148 MW; 38733CE875172E12 CRC64;
MAAAAVAAAA AAAAAASLQV LEMESMETAA AGSAGLAAEV RGSGTVDFGP GPGISAMEAS
GGDPGPEAED FECSSHCSEL SWRQNEQRRQ GLFCDITLCF GGAGGREFRA HRSVLAAATE
YFTPLLSGQF SESRSGRVEM RKWSSEPGPE PDTVEAVIEY MYTGRIRVST GSVHEVLELA
DRFLLIRLKE FCGEFLKKKL HLSNCVAIHS LAHMYTLSQL ALKAADMIRR NFHKVIQDEE
FYTLPFHLIR DWLSDLEITV DSEEVLFETV LKWVQRNAEE RERYFEELFK LLRLSQMKPT
YLTRHVKPER LVANNEVCVK LVADAVERHA LRAENIQSGT CQHPTSHVSL LPRYGQNMDV
IMVIGGVSEG GDYLSECVGY FVDEDRWVNL PHIHNHLDGH AVAVTESYVY VAGSMEPGFA
KTVERYNPNL NTWEHVCSLM TRKHSFGLTE VKGKLYSIGG HGNFSPGFKD VTVYNPELDK
WHNLESAPKI LRDVKALAIE DRFVYIAART PVDRDTEDGL KAVITCYDTE TRQWQDVESL
PLIDNYCFFQ MSVVNSNFYQ TASCCPKSYC LENEEAVRKI ASQVSDEILE SLPPEVLSIE
GAAICYYKDD VFIIGGWKNS DDIDKQYRKE AYRYCAERKR WMLLPPMPQP RCRATACHVR
IPYRYLHGTQ RYPMPQNLMW QKDRIRQMQE IHRHALNMRR VPSSQIEC
