VHLL_HUMAN
ID VHLL_HUMAN Reviewed; 139 AA.
AC Q6RSH7; A1L4M4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=von Hippel-Lindau-like protein;
DE Short=VHL-like protein;
DE Short=VLP;
GN Name=VHLL; Synonyms=VLP;
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 [MRNA], FUNCTION, INTERACTION WITH HIF1A, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF 93-ASN--SER-96.
RX PubMed=14757845;
RA Qi H., Gervais M.L., Li W., DeCaprio J.A., Challis J.R.G., Ohh M.;
RT "Molecular cloning and characterization of the von Hippel-Lindau-like
RT protein.";
RL Mol. Cancer Res. 2:43-52(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Functions as a dominant-negative VHL to serve as a protector
CC of HIFalpha. {ECO:0000269|PubMed:14757845}.
CC -!- SUBUNIT: Interacts via the beta domain with the ODD domain of HIF1A.
CC This interaction is independent of prolyl hydroxylation of HIF1A.
CC {ECO:0000269|PubMed:14757845}.
CC -!- INTERACTION:
CC Q6RSH7; Q15038: DAZAP2; NbExp=8; IntAct=EBI-10254232, EBI-724310;
CC Q6RSH7; Q93062: RBPMS; NbExp=3; IntAct=EBI-10254232, EBI-740322;
CC Q6RSH7; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-10254232, EBI-740343;
CC Q6RSH7; Q08AM6: VAC14; NbExp=3; IntAct=EBI-10254232, EBI-2107455;
CC Q6RSH7; O95231: VENTX; NbExp=3; IntAct=EBI-10254232, EBI-10191303;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the placenta.
CC {ECO:0000269|PubMed:14757845}.
CC -!- MISCELLANEOUS: Has little or no E3 ubiquitin ligase activity as it
CC lacks the alpha domain required for nucleating the multiprotein E3
CC ubiquitin ligase complex.
CC -!- SIMILARITY: Belongs to the VHL family. {ECO:0000305}.
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DR EMBL; AY494836; AAS48916.1; -; mRNA.
DR EMBL; BC130596; AAI30597.1; -; mRNA.
DR EMBL; BC130598; AAI30599.1; -; mRNA.
DR RefSeq; NP_001004319.1; NM_001004319.2.
DR AlphaFoldDB; Q6RSH7; -.
DR SMR; Q6RSH7; -.
DR BioGRID; 133800; 6.
DR IntAct; Q6RSH7; 4.
DR STRING; 9606.ENSP00000464258; -.
DR iPTMnet; Q6RSH7; -.
DR PhosphoSitePlus; Q6RSH7; -.
DR BioMuta; VHLL; -.
DR DMDM; 74749322; -.
DR PaxDb; Q6RSH7; -.
DR PeptideAtlas; Q6RSH7; -.
DR PRIDE; Q6RSH7; -.
DR ProteomicsDB; 67325; -.
DR Antibodypedia; 68434; 56 antibodies from 13 providers.
DR DNASU; 391104; -.
DR Ensembl; ENST00000339922.5; ENSP00000464258.2; ENSG00000189030.10.
DR GeneID; 391104; -.
DR KEGG; hsa:391104; -.
DR MANE-Select; ENST00000339922.5; ENSP00000464258.2; NM_001004319.3; NP_001004319.1.
DR UCSC; uc001fok.4; human.
DR CTD; 391104; -.
DR DisGeNET; 391104; -.
DR GeneCards; VHLL; -.
DR HGNC; HGNC:30666; VHLL.
DR HPA; ENSG00000189030; Tissue enhanced (brain).
DR MIM; 619650; gene.
DR neXtProt; NX_Q6RSH7; -.
DR PharmGKB; PA134987272; -.
DR VEuPathDB; HostDB:ENSG00000189030; -.
DR eggNOG; KOG4710; Eukaryota.
DR GeneTree; ENSGT00390000014353; -.
DR HOGENOM; CLU_1844478_0_0_1; -.
DR InParanoid; Q6RSH7; -.
DR OMA; AGPEEYC; -.
DR OrthoDB; 1509532at2759; -.
DR PhylomeDB; Q6RSH7; -.
DR TreeFam; TF318985; -.
DR PathwayCommons; Q6RSH7; -.
DR SignaLink; Q6RSH7; -.
DR BioGRID-ORCS; 391104; 5 hits in 246 CRISPR screens.
DR GenomeRNAi; 391104; -.
DR Pharos; Q6RSH7; Tdark.
DR PRO; PR:Q6RSH7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6RSH7; protein.
DR Bgee; ENSG00000189030; Expressed in hindlimb stylopod muscle and 33 other tissues.
DR CDD; cd05468; pVHL; 1.
DR Gene3D; 2.60.40.780; -; 1.
DR InterPro; IPR002714; VHL.
DR InterPro; IPR024053; VHL_beta_dom.
DR InterPro; IPR037140; VHL_beta_dom_sf.
DR InterPro; IPR036208; VHL_sf.
DR InterPro; IPR022772; VHL_tumour_suppress_b/a_dom.
DR PANTHER; PTHR15160:SF10; PTHR15160:SF10; 1.
DR Pfam; PF01847; VHL; 1.
DR SUPFAM; SSF49468; SSF49468; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..139
FT /note="von Hippel-Lindau-like protein"
FT /id="PRO_0000265087"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..135
FT /note="Beta-domain"
FT MUTAGEN 93..96
FT /note="NFRS->SYRG: Preferentially binds to a hydroxylated
FT ODD peptide."
FT /evidence="ECO:0000269|PubMed:14757845"
SQ SEQUENCE 139 AA; 15781 MW; 80246038C7F94311 CRC64;
MPWRAGNGVG LEAQAGTQEA GPEEYCQEEL GAEEEMAARA AWPVLRSVNS RELSRIIICN
HSPRIVLPVW LNYYGKLLPY LTLLPGRDFR IHNFRSHPWL FRDARTHDKL LVNQTELFVP
SSNVNGQPVF ANITLQCIP