PRAME_HUMAN
ID PRAME_HUMAN Reviewed; 509 AA.
AC P78395; B2R6Y7; O43481; Q8IXN8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Melanoma antigen preferentially expressed in tumors {ECO:0000305};
DE AltName: Full=Opa-interacting protein 4 {ECO:0000303|PubMed:9466265};
DE Short=OIP-4 {ECO:0000303|PubMed:9466265};
DE AltName: Full=Preferentially expressed antigen of melanoma {ECO:0000303|PubMed:9047241};
GN Name=PRAME {ECO:0000303|PubMed:9047241, ECO:0000312|HGNC:HGNC:9336};
GN Synonyms=MAPE {ECO:0000312|HGNC:HGNC:9336},
GN OIP4 {ECO:0000303|PubMed:9466265};
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], AND TISSUE SPECIFICITY.
RX PubMed=9047241; DOI=10.1016/s1074-7613(00)80426-4;
RA Ikeda H., Lethe B.G., Lehmann F., van Baren N., Baurain J.-F., de Smet C.,
RA Chambost H., Vitale M., Moretta A., Boon T., Coulie P.G.;
RT "Characterization of an antigen that is recognized on a melanoma showing
RT partial HLA loss by CTL expressing an NK inhibitory receptor.";
RL Immunity 6:199-208(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-7.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-7.
RC TISSUE=Brain, Skin, and 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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 452-509.
RX PubMed=9466265; DOI=10.1046/j.1365-2958.1998.00670.x;
RA Williams J.M., Chen G.-C., Zhu L., Rest R.F.;
RT "Using the yeast two-hybrid system to identify human epithelial cell
RT proteins that bind gonococcal Opa proteins: intracellular gonococci bind
RT pyruvate kinase via their Opa proteins and require host pyruvate for
RT growth.";
RL Mol. Microbiol. 27:171-186(1998).
RN [7]
RP FUNCTION IN RETINOIC ACID SIGNALING, INTERACTION WITH EZH2 AND RARA, AND
RP MUTAGENESIS OF 470-LEU-LEU-471.
RX PubMed=16179254; DOI=10.1016/j.cell.2005.07.003;
RA Epping M.T., Wang L., Edel M.J., Carlee L., Hernandez M., Bernards R.;
RT "The human tumor antigen PRAME is a dominant repressor of retinoic acid
RT receptor signaling.";
RL Cell 122:835-847(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16620968; DOI=10.1016/j.leukres.2006.02.031;
RA Proto-Siqueira R., Figueiredo-Pontes L.L., Panepucci R.A., Garcia A.B.,
RA Rizzatti E.G., Nascimento F.M., Ishikawa H.C.F., Larson R.E., Falcao R.P.,
RA Simpson A.J., Gout I., Filonenko V., Rego E.M., Zago M.A.;
RT "PRAME is a membrane and cytoplasmic protein aberrantly expressed in
RT chronic lymphocytic leukemia and mantle cell lymphoma.";
RL Leuk. Res. 30:1333-1339(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, PATHWAY, SUBCELLULAR LOCATION, IDENTIFICATION IN A CRL2 E3
RP UBIQUITIN-PROTEIN LIGASE COMPLEX, AND MUTAGENESIS OF 26-LEU--ALA-30 AND
RP 48-LEU-PRO-49.
RX PubMed=21822215; DOI=10.1038/emboj.2011.262;
RA Costessi A., Mahrour N., Tijchon E., Stunnenberg R., Stoel M.A.,
RA Jansen P.W., Sela D., Martin-Brown S., Washburn M.P., Florens L.,
RA Conaway J.W., Conaway R.C., Stunnenberg H.G.;
RT "The tumour antigen PRAME is a subunit of a Cul2 ubiquitin ligase and
RT associates with active NFY promoters.";
RL EMBO J. 30:3786-3798(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-16, AND
RP IDENTIFICATION BY 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 [12]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN
RP LIGASE COMPLEX.
RX PubMed=23460923; DOI=10.1371/journal.pone.0058052;
RA Wadelin F.R., Fulton J., Collins H.M., Tertipis N., Bottley A.,
RA Spriggs K.A., Falcone F.H., Heery D.M.;
RT "PRAME is a golgi-targeted protein that associates with the Elongin BC
RT complex and is upregulated by interferon-gamma and bacterial PAMPs.";
RL PLoS ONE 8:e58052-e58052(2013).
RN [13]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE
RP COMPLEX.
RX PubMed=26138980; DOI=10.1126/science.aab0515;
RA Lin H.C., Ho S.C., Chen Y.Y., Khoo K.H., Hsu P.H., Yen H.C.;
RT "SELENOPROTEINS. CRL2 aids elimination of truncated selenoproteins produced
RT by failed UGA/Sec decoding.";
RL Science 349:91-95(2015).
CC -!- FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC ubiquitin-protein ligase complex, which mediates ubiquitination of
CC target proteins, leading to their degradation (PubMed:21822215,
CC PubMed:26138980). The CRL2(PRAME) complex mediates ubiquitination and
CC degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed
CC UGA/Sec decoding (PubMed:26138980). In the nucleus, the CRL2(PRAME)
CC complex is recruited to epigenetically and transcriptionally active
CC promoter regions bound by nuclear transcription factor Y (NFY) and
CC probably plays a role in chromstin regulation (PubMed:21822215).
CC Functions as a transcriptional repressor, inhibiting the signaling of
CC retinoic acid through the retinoic acid receptors RARA, RARB and RARG:
CC prevents retinoic acid-induced cell proliferation arrest,
CC differentiation and apoptosis (PubMed:16179254).
CC {ECO:0000269|PubMed:16179254, ECO:0000269|PubMed:21822215,
CC ECO:0000269|PubMed:26138980}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:21822215, ECO:0000269|PubMed:26138980}.
CC -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC PRAME (PubMed:21822215, PubMed:23460923, PubMed:26138980). Interacts
CC with RARA (via the ligand-binding domain); the interaction is direct
CC and ligand (retinoic acid)-dependent (PubMed:16179254). Interacts with
CC EZH2; required to repress RAR signaling (PubMed:16179254).
CC {ECO:0000269|PubMed:16179254, ECO:0000269|PubMed:21822215,
CC ECO:0000269|PubMed:23460923, ECO:0000269|PubMed:26138980}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21822215,
CC ECO:0000269|PubMed:23460923, ECO:0000305|PubMed:16620968}. Chromosome
CC {ECO:0000269|PubMed:21822215}. Cytoplasm {ECO:0000269|PubMed:23460923}.
CC Golgi apparatus {ECO:0000269|PubMed:23460923}. Cell membrane
CC {ECO:0000269|PubMed:16620968}. Note=Associates with chromatin;
CC specifically enriched at transcriptionally active promoters that are
CC also bound by nuclear transcription factor Y (composed of NFYA, NFYB
CC and NFYC) and at enhancers (PubMed:21822215). Recruited to the Golgi
CC apparatus in response to interferon gamma (IFNG) treatment
CC (PubMed:23460923). {ECO:0000269|PubMed:21822215,
CC ECO:0000269|PubMed:23460923}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. Detected in samples of kidney,
CC brain and skin. {ECO:0000269|PubMed:9047241}.
CC -!- INDUCTION: Up-regulated in response to interferon gamma (IFNG)
CC treatment and exposure to bacterial PAMPs (pathogen associated
CC molecular patterns). {ECO:0000269|PubMed:23460923}.
CC -!- MISCELLANEOUS: Tumor antigen recognized by cytolytic T lymphocytes.
CC {ECO:0000269|PubMed:9047241}.
CC -!- SIMILARITY: Belongs to the PRAME family. {ECO:0000305}.
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DR EMBL; U65011; AAC51160.1; -; mRNA.
DR EMBL; CR456549; CAG30435.1; -; mRNA.
DR EMBL; AK312769; BAG35634.1; -; mRNA.
DR EMBL; CH471095; EAW59518.1; -; Genomic_DNA.
DR EMBL; BC014074; AAH14074.1; -; mRNA.
DR EMBL; BC022008; AAH22008.1; -; mRNA.
DR EMBL; BC039731; AAH39731.1; -; mRNA.
DR EMBL; AF025440; AAC39560.1; -; mRNA.
DR CCDS; CCDS13801.1; -.
DR RefSeq; NP_001278644.1; NM_001291715.1.
DR RefSeq; NP_001278645.1; NM_001291716.1.
DR RefSeq; NP_001278646.1; NM_001291717.1.
DR RefSeq; NP_001278648.1; NM_001291719.1.
DR RefSeq; NP_001305055.1; NM_001318126.1.
DR RefSeq; NP_001305056.1; NM_001318127.1.
DR RefSeq; NP_006106.1; NM_006115.4.
DR RefSeq; NP_996836.1; NM_206953.2.
DR RefSeq; NP_996837.1; NM_206954.2.
DR RefSeq; NP_996838.1; NM_206955.2.
DR RefSeq; NP_996839.1; NM_206956.2.
DR AlphaFoldDB; P78395; -.
DR BioGRID; 117078; 141.
DR CORUM; P78395; -.
DR IntAct; P78395; 32.
DR MINT; P78395; -.
DR STRING; 9606.ENSP00000445675; -.
DR iPTMnet; P78395; -.
DR PhosphoSitePlus; P78395; -.
DR BioMuta; PRAME; -.
DR DMDM; 6685631; -.
DR EPD; P78395; -.
DR jPOST; P78395; -.
DR MassIVE; P78395; -.
DR MaxQB; P78395; -.
DR PaxDb; P78395; -.
DR PeptideAtlas; P78395; -.
DR PRIDE; P78395; -.
DR ProteomicsDB; 57611; -.
DR Antibodypedia; 23630; 275 antibodies from 32 providers.
DR DNASU; 23532; -.
DR Ensembl; ENST00000398741.5; ENSP00000381726.1; ENSG00000185686.18.
DR Ensembl; ENST00000398743.6; ENSP00000381728.2; ENSG00000185686.18.
DR Ensembl; ENST00000402697.5; ENSP00000385198.1; ENSG00000185686.18.
DR Ensembl; ENST00000405655.8; ENSP00000384343.3; ENSG00000185686.18.
DR Ensembl; ENST00000539862.2; ENSP00000445097.2; ENSG00000275013.4.
DR Ensembl; ENST00000543184.5; ENSP00000445675.1; ENSG00000185686.18.
DR Ensembl; ENST00000617728.4; ENSP00000484066.1; ENSG00000275013.4.
DR Ensembl; ENST00000626503.2; ENSP00000486485.1; ENSG00000275013.4.
DR Ensembl; ENST00000628830.2; ENSP00000486330.1; ENSG00000275013.4.
DR GeneID; 23532; -.
DR KEGG; hsa:23532; -.
DR MANE-Select; ENST00000405655.8; ENSP00000384343.3; NM_206956.3; NP_996839.1.
DR UCSC; uc032qia.2; human.
DR CTD; 23532; -.
DR DisGeNET; 23532; -.
DR GeneCards; PRAME; -.
DR HGNC; HGNC:9336; PRAME.
DR HPA; ENSG00000185686; Tissue enriched (testis).
DR MIM; 606021; gene.
DR neXtProt; NX_P78395; -.
DR OpenTargets; ENSG00000185686; -.
DR PharmGKB; PA33698; -.
DR VEuPathDB; HostDB:ENSG00000185686; -.
DR eggNOG; ENOG502QWSJ; Eukaryota.
DR GeneTree; ENSGT01030000234531; -.
DR HOGENOM; CLU_039635_2_1_1; -.
DR InParanoid; P78395; -.
DR OMA; TFTFCGN; -.
DR OrthoDB; 631249at2759; -.
DR PhylomeDB; P78395; -.
DR TreeFam; TF332708; -.
DR PathwayCommons; P78395; -.
DR SignaLink; P78395; -.
DR SIGNOR; P78395; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23532; 25 hits in 1083 CRISPR screens.
DR ChiTaRS; PRAME; human.
DR GeneWiki; PRAME; -.
DR GenomeRNAi; 23532; -.
DR Pharos; P78395; Tbio.
DR PRO; PR:P78395; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P78395; protein.
DR Bgee; ENSG00000185686; Expressed in right testis and 84 other tissues.
DR ExpressionAtlas; P78395; baseline and differential.
DR Genevisible; P78395; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IDA:UniProtKB.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IDA:UniProtKB.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR026271; PRAME_family.
DR PIRSF; PIRSF038286; PRAME; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cell membrane; Chromosome; Cytoplasm; Differentiation;
KW Golgi apparatus; Growth regulation; Leucine-rich repeat; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1..509
FT /note="Melanoma antigen preferentially expressed in tumors"
FT /id="PRO_0000156973"
FT REPEAT 116..145
FT /note="LRR 1; degenerate"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 207..231
FT /note="LRR 2; degenerate"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 232..258
FT /note="LRR 3; degenerate"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 259..294
FT /note="LRR 4; degenerate"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 295..320
FT /note="LRR 5"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 321..352
FT /note="LRR 6"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 353..371
FT /note="LRR 7"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 377..404
FT /note="LRR 8"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REPEAT 405..429
FT /note="LRR 9"
FT /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT REGION 416..509
FT /note="Mediates interaction with RARA"
FT /evidence="ECO:0000269|PubMed:16179254"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 7
FT /note="W -> R (in dbSNP:rs1129172)"
FT /evidence="ECO:0000269|PubMed:15461802,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_021258"
FT VARIANT 218
FT /note="M -> V (in dbSNP:rs41277507)"
FT /id="VAR_062137"
FT MUTAGEN 26..30
FT /note="LVELA->PVELF: Impaired formation of the CRL2(PRAME)
FT complex."
FT /evidence="ECO:0000269|PubMed:21822215"
FT MUTAGEN 48..49
FT /note="LP->AA: Impaired formation of the CRL2(PRAME)
FT complex."
FT /evidence="ECO:0000269|PubMed:21822215"
FT MUTAGEN 470..471
FT /note="LL->VV: Loss of interaction with RARA and defective
FT in repressing RARA signaling."
FT /evidence="ECO:0000269|PubMed:16179254"
FT CONFLICT 452
FT /note="H -> D (in Ref. 6; AAC39560)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 57890 MW; B5FFF3E7F7E82606 CRC64;
MERRRLWGSI QSRYISMSVW TSPRRLVELA GQSLLKDEAL AIAALELLPR ELFPPLFMAA
FDGRHSQTLK AMVQAWPFTC LPLGVLMKGQ HLHLETFKAV LDGLDVLLAQ EVRPRRWKLQ
VLDLRKNSHQ DFWTVWSGNR ASLYSFPEPE AAQPMTKKRK VDGLSTEAEQ PFIPVEVLVD
LFLKEGACDE LFSYLIEKVK RKKNVLRLCC KKLKIFAMPM QDIKMILKMV QLDSIEDLEV
TCTWKLPTLA KFSPYLGQMI NLRRLLLSHI HASSYISPEK EEQYIAQFTS QFLSLQCLQA
LYVDSLFFLR GRLDQLLRHV MNPLETLSIT NCRLSEGDVM HLSQSPSVSQ LSVLSLSGVM
LTDVSPEPLQ ALLERASATL QDLVFDECGI TDDQLLALLP SLSHCSQLTT LSFYGNSISI
SALQSLLQHL IGLSNLTHVL YPVPLESYED IHGTLHLERL AYLHARLREL LCELGRPSMV
WLSANPCPHC GDRTFYDPEP ILCPCFMPN
