ENPLL_HUMAN
ID ENPLL_HUMAN Reviewed; 399 AA.
AC Q58FF3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Putative endoplasmin-like protein;
DE AltName: Full=Putative heat shock protein 90 kDa beta member 2;
GN Name=HSP90B2P; Synonyms=GRP94B, GRP94P1, TRAP1;
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].
RX PubMed=16269234; DOI=10.1016/j.ygeno.2005.08.012;
RA Chen B., Piel W.H., Gui L., Bruford E., Monteiro A.;
RT "The HSP90 family of genes in the human genome: insights into their
RT divergence and evolution.";
RL Genomics 86:627-637(2005).
RN [2]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
CC -!- FUNCTION: Putative molecular chaperone. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AY956768; AAX38255.1; -; mRNA.
DR AlphaFoldDB; Q58FF3; -.
DR SMR; Q58FF3; -.
DR IntAct; Q58FF3; 6.
DR GlyGen; Q58FF3; 1 site.
DR iPTMnet; Q58FF3; -.
DR PhosphoSitePlus; Q58FF3; -.
DR SwissPalm; Q58FF3; -.
DR BioMuta; HGNC:12099; -.
DR DMDM; 74706932; -.
DR EPD; Q58FF3; -.
DR jPOST; Q58FF3; -.
DR MassIVE; Q58FF3; -.
DR MaxQB; Q58FF3; -.
DR PeptideAtlas; Q58FF3; -.
DR PRIDE; Q58FF3; -.
DR ProteomicsDB; 62620; -.
DR GeneCards; HSP90B2P; -.
DR HGNC; HGNC:12099; HSP90B2P.
DR neXtProt; NX_Q58FF3; -.
DR InParanoid; Q58FF3; -.
DR PhylomeDB; Q58FF3; -.
DR PathwayCommons; Q58FF3; -.
DR SignaLink; Q58FF3; -.
DR Pharos; Q58FF3; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q58FF3; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 1.20.120.790; -; 1.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF00183; HSP90; 2.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 5: Uncertain;
KW Chaperone; Isopeptide bond; Reference proteome; Stress response;
KW Ubl conjugation.
FT CHAIN 1..399
FT /note="Putative endoplasmin-like protein"
FT /id="PRO_0000349258"
FT REGION 350..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364"
SQ SEQUENCE 399 AA; 45859 MW; 8DB8E2D7E202E3CE CRC64;
MAETIQEVED EYKAFCKSFS KESDDPVACI HFTAEGEVTF KSILFVPTFV PRGLFDEYGS
KKSDYIKLYV RCVFITDDFR DTMPKNLNFV KGVVDSGGLS LNVSCETLQQ HKLLKVIRKK
LVHKTLDMIK KIADEKYNDT FWKEFGTNIK LGVIEDHSNR TCLAKLLRFQ SSHHPADITS
LHQDVERMKE KQDKICLMAG GYEVIYLTEP VVEYCIQALP EFDGKRFQNV AKEGVKFDDS
EKTKESHEAV EKEFEPLPNW VKDKAIKDKI EKAMVSQCLT ESLCALVASQ YGWSGNMERI
MKAQAYQTGK GISTNYHASR KKTFEINPRH PLIRDMLRRI KEDEDDKTVL DLAVVEEPDE
EPEETAEDKE QDKDKEMDVG TDEEKQETAK ESTAEKDEL