RNF6_HUMAN
ID RNF6_HUMAN Reviewed; 685 AA.
AC Q9Y252; B4DDP0; Q5W0H0; Q9BZP5; Q9UF41;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=E3 ubiquitin-protein ligase RNF6;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF6 {ECO:0000305};
GN Name=RNF6; Synonyms=SPG2;
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] (ISOFORM 1).
RC TISSUE=Leukocyte;
RX PubMed=10331950; DOI=10.1006/geno.1999.5802;
RA Macdonald D.H.C., Lahiri D., Sampath A., Chase A., Sohal J., Cross N.C.P.;
RT "Cloning and characterization of RNF6, a novel RING finger gene mapping to
RT 13q12.";
RL Genomics 58:94-97(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RA Alao J.P., Grand F.H., MacDonald D.H.C.;
RT "Alternative splice variant of the RING-H2 protein RNF6 lacks the RING-H2
RT domain.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=18368307; DOI=10.1007/s11427-008-0047-3;
RA Zhu L., Tong G., Chen J., Wang Y., Wang S., Zhao M., Li J., Ma J.;
RT "Cloning and identification of a novel RNF6 transcriptional splice variant
RT Spg2 in human development.";
RL Sci. China, Ser. C, Life Sci. 51:302-307(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 320-685 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP FUNCTION, INTERACTION WITH AR, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19345326; DOI=10.1016/j.ccr.2009.02.021;
RA Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z., Chen H.,
RA Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z., Veenstra T.D.,
RA Qiu Y.;
RT "Regulation of androgen receptor transcriptional activity and specificity
RT by RNF6-induced ubiquitination.";
RL Cancer Cell 15:270-282(2009).
RN [10]
RP INVOLVEMENT IN ESCR, AND VARIANTS SER-48; LYS-102; THR-164; THR-242;
RP ASP-244; GLN-572 AND ASN-623.
RX PubMed=12154016;
RA Lo H.S., Hu N., Gere S., Lu N., Su H., Goldstein A.M., Taylor P.R.,
RA Lee M.P.;
RT "Identification of somatic mutations of the RNF6 gene in human esophageal
RT squamous cell carcinoma.";
RL Cancer Res. 62:4191-4193(2002).
CC -!- FUNCTION: E3 ubiquitin-protein ligase mediating 'Lys-48'-linked
CC polyubiquitination of LIMK1 and its subsequent targeting to the
CC proteasome for degradation. Negatively regulates axonal outgrowth
CC through regulation of the LIMK1 turnover. Mediates 'Lys-6' and 'Lys-
CC 27'-linked polyubiquitination of AR/androgen receptor thereby
CC modulating its transcriptional activity. May also bind DNA and function
CC as a transcriptional regulator. {ECO:0000269|PubMed:19345326}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with LIMK1 (By similarity). Interacts with AR.
CC {ECO:0000250, ECO:0000269|PubMed:19345326}.
CC -!- INTERACTION:
CC Q9Y252; P10275: AR; NbExp=10; IntAct=EBI-2341483, EBI-608057;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19345326}. Cytoplasm
CC {ECO:0000269|PubMed:19345326}. Cell projection, axon {ECO:0000250}.
CC Nucleus, PML body {ECO:0000250}. Note=Localizes to the PML nuclear
CC bodies in Sertoli cells. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y252-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y252-2; Sequence=VSP_055424, VSP_055425;
CC Name=3;
CC IsoId=Q9Y252-3; Sequence=VSP_055426, VSP_055427;
CC -!- TISSUE SPECIFICITY: Weakly expressed in peripheral blood, spleen,
CC prostate, testis and ovary. According to PubMed:18368307, it is
CC preferentially expressed in testis and ovary and hardly detected in
CC other tissues. {ECO:0000269|PubMed:18368307,
CC ECO:0000269|PubMed:19345326}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo and adult testis.
CC {ECO:0000269|PubMed:18368307}.
CC -!- DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the
CC esophagus. The most common types are esophageal squamous cell carcinoma
CC and adenocarcinoma. Cancer of the esophagus remains a devastating
CC disease because it is usually not detected until it has progressed to
CC an advanced incurable stage. {ECO:0000269|PubMed:12154016}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- MISCELLANEOUS: Required for prostate tumor cell growth.
CC -!- SIMILARITY: Belongs to the RNF12 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ010347; CAB40414.1; -; mRNA.
DR EMBL; AJ010346; CAB40413.1; -; mRNA.
DR EMBL; AF293342; AAK00848.1; -; mRNA.
DR EMBL; AY009109; AAG49400.1; -; mRNA.
DR EMBL; AK293272; BAG56801.1; -; mRNA.
DR EMBL; AK312435; BAG35344.1; -; mRNA.
DR EMBL; AL138966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08380.1; -; Genomic_DNA.
DR EMBL; BC034688; AAH34688.1; -; mRNA.
DR EMBL; AL133621; CAB63747.1; -; mRNA.
DR CCDS; CCDS9316.1; -. [Q9Y252-1]
DR PIR; T43459; T43459.
DR RefSeq; NP_005968.1; NM_005977.3. [Q9Y252-1]
DR RefSeq; NP_898864.1; NM_183043.2. [Q9Y252-1]
DR RefSeq; NP_898865.1; NM_183044.2. [Q9Y252-1]
DR RefSeq; NP_898866.1; NM_183045.1. [Q9Y252-3]
DR RefSeq; XP_005266542.1; XM_005266485.2. [Q9Y252-1]
DR RefSeq; XP_005266543.1; XM_005266486.2. [Q9Y252-1]
DR RefSeq; XP_011533479.1; XM_011535177.2. [Q9Y252-1]
DR RefSeq; XP_011533480.1; XM_011535178.1. [Q9Y252-3]
DR AlphaFoldDB; Q9Y252; -.
DR SMR; Q9Y252; -.
DR BioGRID; 111976; 71.
DR IntAct; Q9Y252; 7.
DR STRING; 9606.ENSP00000371000; -.
DR iPTMnet; Q9Y252; -.
DR PhosphoSitePlus; Q9Y252; -.
DR BioMuta; RNF6; -.
DR DMDM; 13124536; -.
DR EPD; Q9Y252; -.
DR jPOST; Q9Y252; -.
DR MassIVE; Q9Y252; -.
DR MaxQB; Q9Y252; -.
DR PaxDb; Q9Y252; -.
DR PeptideAtlas; Q9Y252; -.
DR PRIDE; Q9Y252; -.
DR ProteomicsDB; 85654; -. [Q9Y252-1]
DR Antibodypedia; 35204; 254 antibodies from 30 providers.
DR DNASU; 6049; -.
DR Ensembl; ENST00000346166.7; ENSP00000342121.3; ENSG00000127870.17. [Q9Y252-1]
DR Ensembl; ENST00000381570.7; ENSP00000370982.3; ENSG00000127870.17. [Q9Y252-1]
DR Ensembl; ENST00000381588.9; ENSP00000371000.4; ENSG00000127870.17. [Q9Y252-1]
DR GeneID; 6049; -.
DR KEGG; hsa:6049; -.
DR MANE-Select; ENST00000381588.9; ENSP00000371000.4; NM_005977.4; NP_005968.1.
DR UCSC; uc001uqo.4; human. [Q9Y252-1]
DR CTD; 6049; -.
DR DisGeNET; 6049; -.
DR GeneCards; RNF6; -.
DR HGNC; HGNC:10069; RNF6.
DR HPA; ENSG00000127870; Low tissue specificity.
DR MalaCards; RNF6; -.
DR MIM; 133239; phenotype.
DR MIM; 604242; gene.
DR neXtProt; NX_Q9Y252; -.
DR OpenTargets; ENSG00000127870; -.
DR Orphanet; 99977; Squamous cell carcinoma of the esophagus.
DR PharmGKB; PA34443; -.
DR VEuPathDB; HostDB:ENSG00000127870; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000158530; -.
DR HOGENOM; CLU_025933_0_0_1; -.
DR InParanoid; Q9Y252; -.
DR OMA; HLPEMHS; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q9Y252; -.
DR TreeFam; TF325756; -.
DR PathwayCommons; Q9Y252; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9Y252; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 6049; 11 hits in 1120 CRISPR screens.
DR ChiTaRS; RNF6; human.
DR GenomeRNAi; 6049; -.
DR Pharos; Q9Y252; Tbio.
DR PRO; PR:Q9Y252; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y252; protein.
DR Bgee; ENSG00000127870; Expressed in bronchial epithelial cell and 207 other tissues.
DR ExpressionAtlas; Q9Y252; baseline and differential.
DR Genevisible; Q9Y252; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:UniProtKB.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..685
FT /note="E3 ubiquitin-protein ligase RNF6"
FT /id="PRO_0000056047"
FT ZN_FING 632..673
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..685
FT /note="Required for polyubiquitination"
FT /evidence="ECO:0000250"
FT COMPBIAS 12..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..15
FT /note="MNQSRSRSDGGSEET -> MQLEVDKMGTKLGEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055424"
FT VAR_SEQ 16..371
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055425"
FT VAR_SEQ 137..142
FT /note="VSRTNP -> ALPDTS (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055426"
FT VAR_SEQ 143..685
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_055427"
FT VARIANT 48
FT /note="N -> S (in dbSNP:rs3910433)"
FT /evidence="ECO:0000269|PubMed:12154016"
FT /id="VAR_034465"
FT VARIANT 102
FT /note="R -> K (found in an esophageal cancer sample;
FT esophageal squamous cell carcinoma; somatic mutation;
FT dbSNP:rs121434522)"
FT /evidence="ECO:0000269|PubMed:12154016"
FT /id="VAR_063490"
FT VARIANT 164
FT /note="I -> T (in dbSNP:rs61760897)"
FT /evidence="ECO:0000269|PubMed:12154016"
FT /id="VAR_063491"
FT VARIANT 203
FT /note="V -> E (in dbSNP:rs7990167)"
FT /id="VAR_052094"
FT VARIANT 242
FT /note="A -> T (found in an esophageal cancer sample;
FT esophageal squamous cell carcinoma; somatic mutation;
FT dbSNP:rs121434523)"
FT /evidence="ECO:0000269|PubMed:12154016"
FT /id="VAR_063492"
FT VARIANT 244
FT /note="G -> D (found in an esophageal cancer sample;
FT esophageal squamous cell carcinoma; somatic mutation;
FT dbSNP:rs121434524)"
FT /evidence="ECO:0000269|PubMed:12154016"
FT /id="VAR_063493"
FT VARIANT 572
FT /note="R -> Q (in dbSNP:rs138379662)"
FT /evidence="ECO:0000269|PubMed:12154016"
FT /id="VAR_063494"
FT VARIANT 623
FT /note="S -> N (in dbSNP:rs17083436)"
FT /evidence="ECO:0000269|PubMed:12154016"
FT /id="VAR_052095"
SQ SEQUENCE 685 AA; 78091 MW; 344584773F2E5EFC CRC64;
MNQSRSRSDG GSEETLPQDH NHHENERRWQ QERLHREEAY YQFINELNDE DYRLMRDHNL
LGTPGEITSE ELQQRLDGVK EQLASQPDLR DGTNYRDSEV PRESSHEDSL LEWLNTFRRT
GNATRSGQNG NQTWRAVSRT NPNNGEFRFS LEIHVNHENR GFEIHGEDYT DIPLSDSNRD
HTANRQQRST SPVARRTRSQ TSVNFNGSSS NIPRTRLASR GQNPAEGSFS TLGRLRNGIG
GAAGIPRANA SRTNFSSHTN QSGGSELRQR EGQRFGAAHV WENGARSNVT VRNTNQRLEP
IRLRSTSNSR SRSPIQRQSG TVYHNSQRES RPVQQTTRRS VRRRGRTRVF LEQDRERERR
GTAYTPFSNS RLVSRITVEE GEESSRSSTA VRRHPTITLD LQVRRIRPGE NRDRDSIANR
TRSRVGLAEN TVTIESNSGG FRRTISRLER SGIRTYVSTI TVPLRRISEN ELVEPSSVAL
RSILRQIMTG FGELSSLMEA DSESELQRNG QHLPDMHSEL SNLGTDNNRS QHREGSSQDR
QAQGDSTEMH GENETTQPHT RNSDSRGGRQ LRNPNNLVET GTLPILRLAH FFLLNESDDD
DRIRGLTKEQ IDNLSTRHYE HNSIDSELGK ICSVCISDYV TGNKLRQLPC MHEFHIHCID
RWLSENCTCP ICRQPVLGSN IANNG
